Table S1. Structural parameters of 152 protein-RNA complexes (classified into four different class based on the type of RNA associated with the protein). Column headers: 1: Reference (references are unavailable for two PDB ids 1ZBH and 3QJJ). 2: PDB id of the protein-RNA complex 3-4: Protein and RNA components of the complex with length of the protein chain and the RNA chain are in parentheses. 5. Resolution of the X-ray structure. 6-7: Chain ids in the PDB entry. Symmetry-related chains are primed (e.g. A' in 1J1U). 8-10: Total buried surface area (B), area of the protein surface and RNA surface buried in the complex. 11-12: Number of interface amino acid residues and interface nucleotides. 13-14: f_np: percent fraction of the B contributed by non-polar (carbon containing) groups on the protein and the RNA side of the interface. 15-16: f_bu: percent fraction of the interface protein and the RNA atoms that are buried (zero SASA) in the complex. 17-18: LD: packing density index as defined by equation 5 in the text. 19: N_hb: number of H-bonds between aminoacids and nucleotides at the protein-RNA interface. 20: SB: number of salt bridges at protein-RNA interface. 21: Sc: shape complementarity index of the protein-RNA complex. 22: GV: mean gap volume index of the protein-RNA complex. 1 Ref. PDB id Composition Pro Res (Å) RNA B (Å2) Chain id Pro RNA 2.9 A R 2.6 P 2.4 Tot Interface residues/nt Pro RNA f_np Pro f_bu RNA Pro LD RNA Pro N_ hb SB Sc GV (Å) Pro RNA RNA 4432 2130 2302 82 31 55 28 32 28 48 47 25 6 0.58 8 R 2617 1235 1382 53 18 56 33 23 24 38 39 19 6 0.58 10 A B 4504 2178 2326 73 32 53 34 33 35 45 48 44 13 0.74 9 2.2 A B 5769 2663 3106 98 40 59 38 28 20 45 44 41 11 0.67 7 2.2 A T 4971 2463 2508 80 37 51 34 24 22 42 43 32 13 0.62 3 2.9 A C 5173 2502 2671 100 41 55 34 24 24 35 40 28 11 0.60 1 2.9 AA' B 3759 1797 1962 68 29 54 27 19 20 38 36 26 15 0.67 2 2.9 AB T 2481 1155 1325 39 18 63 31 30 24 41 47 17 6 0.71 20 tRNA-Tyr (77) 2.0 AA' B 2242 1065 1177 41 18 51 35 23 23 32 31 19 3 0.75 16 tRNA-Glu (75) 2.1 A C 4511 2120 2390 86 32 59 34 27 26 41 44 34 13 0.65 6 tRNA-Thr (76) 2.9 A B 4603 2268 2335 78 28 56 35 25 26 38 46 29 8 0.62 9 tRNA-Gln (75) 2.3 A B 5203 2427 2775 85 35 53 32 25 25 40 52 38 21 0.67 6 2.9 AB T 2292 1142 1150 40 18 48 31 17 19 25 28 13 10 0.67 20 2.3 B A 4558 2152 2406 85 32 54 37 27 29 43 45 28 10 0.60 6 A. tRNA (31) [1] 1ASY [2] 1B23 [3] 1C0A [4] 1F7U [5] 1FFY [6] 1GAX [7] 1H3E [8] 1H4S [9] 1J1U [10] 1N78 [11] 1QF6 [12] 1QTQ [13] [14] 1SER 1U0B Yeast aspartyltRNA synthetase (490) T. Aquaticus EF-TU (405) E. coli aspartyltRNA synthetase (585) Arginyl-tRNA synthetase (607) Isoleucyl-tRNA synthetase (917) Valyl-tRNA synthetase (862) T. thermophilus tyrosyl-tRNA synthetase (432) T. thermophilus prolyl-tRNA synthetase (477+477) M. jannaschii Tyrosyl-tRNA synthetase (306+306) T. thermophilus glutamyl-tRNA synthetase (468) E. coli threonyltRNA synthetase (642) E. Coli GlutaminyltRNA synthetase (553) T. thermophilusser yl-tRNA synthetase (421+421) E.coli cysteinyltRNA tRNA-Asp (75) E. coli tRNA-Cys (74) tRNA-Asp (77) tRNA-Arg (76) tRNA-Ile (75) tRNA-Val (75) tRNA-Tyr (86) tRNA-Pro (77) tRNA-Ser (94) tRNA-Cys (74) 2 [15] 1VFG [16] 2AZX [17] 2CSX [18] 2DLC [19] 2DRB [20] 2DU3 [21] 2FK6 [22] 2FMT synthetase (461) CCA-adding enzyme (390) H. sapiens tryptophanyltRNA synthetase (477) MethionyltRNA synthetase (497) Tyrosyl-tRNA synthetase(394) CCA-adding enzyme (437) OphosphoseryltRNA synthetase(534+ 534+534+534) RNase Z (320) MethionyltRNAfmet transformylase (314) Isopentenyltrans ferase (316) Arginyl-tRNA synthetase (629) [23] 2ZM5 [24] 2ZUE [25] 2ZZM [26] 3ADB [27] 3AMT [28] 3EPH [29] 3HL2 Trm5 (336) OphosphoseryltRNA kinase (259) Agmatinylcytidi ne synthetase TiaS (440) DMATase (409) Selenium transferase (501) [30] [31] 3VJR 3ZJT Peptidyl-tRNA hydrolase (197) E.coli leucyl- tRNA (75) 2.8 B D 1665 833 832 39 15 48 35 11 10 22 30 11 4 0.66 16 tRNA-Trp (75) 2.8 AA' C 2134 1023 1111 40 18 55 27 26 23 32 35 19 4 0.67 20 2.7 A C 2183 1041 1142 42 22 47 37 32 33 40 43 18 3 0.69 16 2.4 XX' YY' 4266 2056 2210 72 30 55 36 25 28 34 36 30 4 0.70 13 2.8 A B 3198 1449 1749 60 18 52 34 35 36 40 48 30 14 0.70 8 2.6 AA' BB' DD' 2812 1296 1516 58 30 61 26 24 19 34 32 12 4 0.78 9 2.9 A R 1531 751 781 23 17 61 39 20 20 27 29 5 8 0.68 14 2.8 A C 2941 1499 1442 43 25 55 33 20 23 35 46 27 9 0.68 8 2.6 A C 3937 1953 1983 61 20 56 34 23 29 51 71 32 20 0.64 6 2.0 A B 4934 2366 2568 85 38 58 34 30 21 41 41 27 10 0.64 9 2.7 A B 4524 2138 2386 77 30 57 33 25 28 48 51 37 21 0.66 6 2.8 A C 3099 1579 1521 51 28 57 30 10 14 28 37 14 15 0.57 10 2.9 A B 3822 1826 1996 66 26 48 31 32 26 50 49 27 14 0.68 8 3.0 A E 4815 2298 2517 80 27 51 31 30 34 52 69 38 24 0.65 6 2.8 AA' BB' E 2186 1092 1094 38 20 50 35 16 18 27 28 15 10 0.61 9 2.4 2.2 A A B B 1355 4323 690 2125 664 2197 21 77 15 35 59 57 32 35 15 14 23 19 25 30 33 32 9 18 4 16 0.61 0.58 9 12 tRNA-Met (75) tRNA-Tyr (76) tRNAmini CCA (35) tRNA-Cys (71+71) tRNA-Thr (79) tRNAfmet (77) tRNA-Phe (76) tRNA-Arg (78) tRNA-Leu (84) tRNA-Sec (92) tRNA-Ile (78) tRNA-Cys (69) tRNA-Sec (90) tRNA CCAacceptor (36) tRNA-Leu 3 tRNA synthetase (880) (88) Ribosomal protein L25 (94) Ribosomal protein L5 (206) Ribosomal proteins S15, S6, S18 (98+88+88) M. jannaschii ribosomal protein S8 (130) T. thermophilus ribosomal protein L5 (182) T. maritima ribosomal protein L11 (140) S. acidocaldarius ribosomal protein L1P (217) E. coli ribosomal protein S8 (129) 50S ribosomal protein L7Ae (117) Ribosomal protein L1 (228) 5s rRNA (19+19) 5s rRNA (19+21) dsRBD A (69+69) dsRNA (10+10) 4.5S RNA domain IV (49) RNA transcript (10) B. Ribosomal (10) [32] 1DFU [33] 1FEU [34] 1G1X [35] 1I6U [36] 1MJI [37] 1MMS [38] 1MZP [39] 1S03 [40] 1SDS [41] 2HW8 C. Duplex (49) [42] 1DI2 [43] 1HQ1 [44] 1MSW [45] 1N35 [46] 1OOA E.coli SRP (105) T7 RNA polymerase (883) Reovirus polymerase (1267) NF-kappaB p50 (326) 1.8 P MN 1688 828 860 26 19 47 21 29 32 42 41 17 14 0.67 5 2.3 A BC 1595 790 806 26 18 40 28 37 41 37 36 24 12 0.71 9 2.6 ABC DE 4945 2427 2518 73 47 57 28 35 32 43 44 36 22 0.65 5 2.6 A C 1802 885 916 30 19 55 39 33 25 40 40 16 5 0.56 6 2.5 A C 1745 878 867 30 17 49 39 24 28 35 38 6 2 0.53 7 2.6 A C 2455 1200 1255 37 23 52 31 37 39 40 44 24 14 0.73 5 2.7 A B 2949 1511 1437 39 27 49 27 33 39 40 51 32 23 0.69 5 RNA (47) box H/ACA sRNA (15) 2.7 H A 1744 848 896 29 16 61 36 24 20 40 41 11 3 0.62 8 1.8 C FF' 1200 553 647 21 8 56 25 32 27 32 43 15 6 0.74 6 mRNA (36) 2.1 A B 2401 1164 1237 36 21 69 31 48 48 49 48 19 3 0.64 6 1.9 AB DE 1840 933 907 30 16 53 30 18 18 25 30 16 5 0.72 4 1.5 A B 1365 688 676 20 13 54 35 44 47 39 43 15 4 0.77 8 2.1 D R 1828 902 926 40 10 55 38 11 17 22 33 7 2 0.63 25 2.5 A BC 3245 1558 1686 72 13 59 30 31 27 41 55 14 4 0.53 17 2.5 A C 1910 997 913 29 19 51 19 23 20 37 43 17 4 0.60 9 16S rRNA (41+44) 16S rRNA (37) 5S rRNA fragment (34) T. maritima 23S rRNA fragment (58) 23S rRNA fragment (55) dsRNA (5+10) aptamer RNA (29) 4 [47] 1Q2R [48] 1R3E [49] 1R9F [50] 1SI3 [51] 1WNE [52] 1YVP [53] 1ZBI [54] 2AZ0 [55] 2BGG [56] 2EZ6 [57] 2F8S [58] 2GJW [59] 2GXB [60] 2OZB [61] 2PJP [62] 2QUX Guanine transglycosylase (386+386) Pseudouridine Synthase TruB (309) p19 (136+136) PAZ domain of eIF2c1 (149) Foot-and-mouth disease virus polymerase (476) Ro autoantigen (538) RNase H (142+142) Flock house virus B2 (73+73) A. fulgidus PIWI (427) RNase III (221+221) A. aeolicus Argonaute (706+706) Splicing endonuclease (313+313) Z alpha domain of adenosine deaminase (66) Ribonucleoprot ein (130+260) E.coli SelB (121) Pseudomonas phage PP7 coat protein (125+125) 20-mer tRNA fragment (20) tRNA fragment ( 17) siRNA (21+21) siRNA (9) templateprimer RNA decanucleot ide (8+5) Y RNA (10+10+10) A form RNA (12+12) siRNA (18+18) siRNA (8+8) 28-mer RNA (28+28) siRNA (22+22) bulgehelix-bulge RNA (19+12+7) dsRNA (7+7) U4snRNA (33) SECIS RNA (23 mer) hairpin RNA (25) 2.9 AB E 3007 1417 1590 52 16 43 36 34 31 41 55 29 7 0.64 8 2.1 A C 3683 1716 1968 60 23 52 29 36 34 56 64 30 15 0.63 3 1.9 AA' BC 3217 1535 1682 56 25 62 43 25 22 35 38 20 15 0.66 5 2.6 A B 1594 765 828 28 9 46 31 28 23 38 40 15 10 0.68 4 3.0 A BC 3079 1427 1652 58 13 53 33 37 38 42 61 17 6 0.62 6 2.2 B EFH 4208 1987 2221 75 21 54 30 30 35 48 47 39 6 0.68 6 1.9 A CD 1675 790 885 29 12 41 30 34 47 42 49 15 2 0.69 3 2.6 AB CD 2264 1103 1161 30 18 57 36 30 33 38 38 22 8 0.69 4 2.2 A PQ 2241 1027 1214 36 11 51 34 37 33 41 55 20 9 0.73 7 2.1 AB CD 5194 2617 2577 83 44 55 36 25 26 34 41 45 10 0.66 6 3.0 AB CD 990 488 502 20 6 52 40 18 16 28 43 2 2 0.74 33 2.9 AB EFH 3244 1525 1718 57 19 56 40 39 31 52 51 14 12 0.62 10 2.3 A EF 769 363 406 12 7 62 24 29 30 35 32 5 3 0.76 5 2.6 AB C 2569 1261 1308 42 17 58 28 26 33 37 61 24 12 0.61 8 2.3 A B 1300 628 673 21 8 40 26 31 31 34 29 16 11 0.76 5 2.4 AB C 1754 801 953 35 11 38 29 22 29 28 35 26 5 0.77 8 5 synthetic FAB (214+224) [63] 2R8S [64] 2XD0 [65] 2Y8W P. atrosepticum ToxN (171) Endoribonuclea se Cse3 (215) [66] 2YKG RIG-I (696) [67] 2ZI0 [68] 2ZKO TAV2b (75+75) NS1 protein of influenza A (73+73) [69] 3A6P [70] 3BSN Exp-5:RanGTP (1024+13+216) Norwalk virus polymerase (510) [71] 3BT7 Methyltransfera se TrmA (369) [72] 3DD2 Thrombin (258) [73] 3DH3 [74] 3EQT [75] 3FTE RluF (290) Helicase DHX58 (145) Methyltransfera se KsgA (249) [76] 3IAB [77] 3KS8 [78] 3MOJ [79] 3O3I [80] [81] 3OIJ 3OL6 RNases P/MRP (158+140) Polymerase cofactor VP35 (184+184) Helicase dbpA (76) Hiwi1 PAZ domain (124) Methyltransfera se (253+253) Poliovirus ribozyme (159) P. atrosepticu m ToxI (36) hairpin RNA (20) dsRNA (10+10) siRNA (21+21) A-form dsRNA (21+21) premicroRNA (24+24) 2.0 LH R 2510 1194 1316 42 27 53 33 29 22 48 40 25 2 0.71 22 3.0 A G 1887 882 1005 35 15 59 28 29 24 39 36 8 3 0.53 6 1.8 A B 3258 1528 1730 50 17 46 28 30 27 51 51 44 20 0.72 3 2.5 A CD 2150 985 1165 45 16 70 35 22 24 31 39 13 3 0.68 19 2.8 AB CD 4574 2341 2234 54 39 44 17 18 23 39 43 41 43 0.70 3 1.7 AB CD 2466 1238 1228 34 20 65 36 16 31 40 47 16 18 0.62 6 2.9 ABC DE 4223 2043 2180 77 34 52 37 19 19 35 39 14 18 0.53 17 RNA (8+9) T-arm analogue (19) 26-mer RNA (26) 23S RNA (22) 1.8 A PT 3112 1448 1663 71 17 59 27 20 22 38 43 22 9 0.61 7 2.4 A C 2230 982 1249 42 12 48 33 32 32 47 53 30 7 0.58 8 1.9 H B 1823 892 931 26 15 44 28 20 25 35 48 17 7 0.70 7 3.0 B F 3425 1664 1761 56 18 42 27 38 45 60 71 44 19 0.67 4 dsRNA (8) rRNA (22+22) RNase MRP P3 domain (46) 2.0 AB CD 2706 1216 1490 48 16 66 35 33 40 38 52 24 8 0.69 5 3.0 A CD 837 429 407 17 13 63 37 7 9 15 24 2 3 0.46 24 2.7 AB R 5088 2387 2701 81 29 62 32 34 32 55 60 35 11 0.70 3 2.4 AB EF 1664 799 864 32 12 54 35 19 26 34 46 11 10 0.59 9 2.9 B A 1759 857 902 27 15 58 31 32 22 38 40 13 8 0.70 8 2.8 X A 923 405 518 20 5 50 30 45 40 41 37 14 0 0.71 6 3.0 2.5 AB A C BCD 2070 4175 999 1999 1072 2176 35 79 10 22 50 59 37 32 39 24 48 26 47 42 63 52 22 23 7 12 0.77 0.56 10 6 dsRNA (18+18) E.coli 23S rRNA fragment (74) piRNA (14) SSU rRNA (14+14) RNA 6 [82] 3RW6 [83] 3SNP [84] 3ZC0 [85] 4ATO [86] 4ERD polymerase (471) Nuclear RNA export factor 1 (267) Iron regulatory protein 1 (908) A. fulgidus C3PO (199+199+199+ 199+199+199+ 199+199) B. thuringiensis ToxN (194+194+194) p65 C-terminal domain (129+129) Exonuclease [87] 4FVU (243) Oligoadenylate synthetase 1 [88] 4IG8 (349) Endoribonuclea se Cas6 [89] 4ILL (289+289) Bacteriophage Qβ coat protein [90] 4L8H (132+132) D. Single-stranded (62) Cap-specific mRNA methyltransfera [91] 1AV6 se (295) [92] 1C9S TRAP (74) poly(A)-binding [93] 1CVJ protein (190) RRMdomain of the HuD protein (167) [94] 1G2E Restrictocin (149) [95] 1JBS H. sapiens [96] 1JID SRP19 (128) (26+14+9) CTE RNA (62) ferritin H IRE RNA (30) duplex RNA (16+16) B. thuringiensi s ToxI (34) stem IV of telomerase RNA (22+22) dsRNA (8+8) dsRNA (18+18) CRISPR RNA (24+24) operator hairpin RNA (20) M7G capped RNA (6) ssRNA (7) polyA (11) class II ARE fragment (10) SRD RNA Analogue (29 mer) SRP RNA (29) 2.3 A H 2699 1319 1380 44 28 54 38 23 25 39 38 10 3 0.61 8 2.8 A C 2872 1351 1522 60 18 50 34 28 30 38 45 23 6 0.63 13 3.0 AA' BB'C C'D D' MM' 2324 1123 1201 48 18 37 21 3 15 28 40 14 22 0.64 39 2.2 A G 2265 1104 1161 33 12 51 30 23 32 45 49 26 10 0.74 5 2.6 AB CD 3281 1590 1690 47 18 66 38 26 44 39 48 20 13 0.69 6 2.9 A BC 1240 575 666 24 9 42 34 30 35 37 44 10 2 0.59 8 2.7 A BC 2914 1416 1499 48 20 50 35 26 25 41 43 26 10 0.58 7 2.5 AB RC 7076 3272 3804 115 33 53 32 34 34 50 62 53 28 0.66 4 2.4 AB R 1995 914 1081 33 12 43 32 22 20 36 37 17 11 0.66 6 2.8 1.9 A L B W1-7 845 1028 385 487 460 541 19 18 4 6 60 58 32 33 22 39 28 29 30 40 38 39 5 8 3 0 0.61 0.79 14 3 2.6 A M 2823 1196 1626 48 9 51 39 44 33 56 53 24 4 0.73 2 2.3 A B 2776 1322 1454 45 10 55 35 33 34 49 59 17 8 0.69 3 2.0 A C 1313 668 645 28 14 51 35 14 20 25 37 8 7 0.70 7 1.8 A B 1436 703 733 26 10 48 23 27 20 29 38 17 19 0.76 6 7 [97] 1K8W [98] 1KNZ [99] 1KQ2 [100] 1LNG [101] 1M5O [102] 1M8V [103] 1M8W [104] 1UVI [105] 1WPU [106] 1WSU NA 1ZBH [107] 1ZH5 [108] 2A8V [109] [110] 2ANR 2ASB [111] 2B3J [112] [113] 2BH2 2BX2 [114] 2DB3 Pseudouridine synthase B (327) Rotavirus NSP3 (164) Hfq (77+77+77+77+ 77+77) M. jannaschii SRP19 (87) U1 Snp (100) P. abyssi Sm PROTEIN (77+77) Pumiliohomology domain (349) phi6 RNA polymerase (664) HutP antitermination protein (147) Elongation Factor SelB (124) exonuclease ERI1 (299+299) La autoantigen (195+195) RHO (118) Nova-1 KH1/KH2 domain (178) Nus A (251) TadA (159) Methyltransfera se RumA (433) RNase E (517) DEAD-box helicase vasa T stemloop RNA (22) 1.9 A B 2974 1342 1632 49 13 56 28 44 45 57 75 26 9 0.65 4 mRNA (5) 2.5 AB W 1921 762 1159 40 5 50 36 47 54 59 61 30 7 0.74 5 2.7 ABH IKM R 3026 1354 1672 44 7 73 38 48 46 60 70 14 0 0.60 5 2.3 A B 2368 1145 1223 30 22 56 22 33 31 40 44 29 18 0.67 9 2.2 C B 1767 822 944 29 13 52 30 34 29 46 43 18 3 0.79 10 2.6 AM O 1289 603 687 22 6 65 40 28 26 30 53 6 2 0.74 4 Nre1-19 RNA (8+8) 2.2 A CE 2142 973 1169 38 14 45 39 35 45 37 70 27 1 0.71 5 6-mer RNA (6) 2.2 A D 1814 780 1034 46 4 53 41 41 43 49 49 7 2 0.59 14 1.5 A C 1358 623 735 27 7 73 45 47 35 48 46 9 0 0.71 4 2.3 A E 938 452 486 13 6 51 23 26 32 28 34 11 8 0.71 8 3.0 AD E 1756 886 870 27 12 54 30 16 19 31 43 7 7 0.67 16 1.9 AB C 1849 830 1020 32 9 65 38 27 25 33 37 8 1 0.69 13 2.4 B E 719 281 438 17 4 78 35 45 33 41 33 6 0 0.79 7 1.9 1.5 A A B B 1220 2317 583 1092 636 1225 21 40 10 11 66 69 33 43 40 46 32 37 34 44 50 53 10 17 3 1 0.70 0.75 7 4 2.0 AB E 2099 1007 1092 40 10 53 43 39 47 50 67 20 9 0.62 5 2.2 2.9 A L C R 4492 912 2153 419 2339 493 78 22 25 4 48 57 32 32 30 27 32 20 49 35 57 37 40 4 16 4 0.70 0.66 4 29 2.2 A E 1193 494 699 26 6 56 19 43 37 37 44 20 6 0.73 16 7-mer RNA (7) 7S SRP RNA (97) Hairpin ribozyme (92) Uridine Heptamer (7) hut mRNA (7) SECIS RNA (23 mer) Histone mRNA (20 mer) 3'-terminii mRNA (9) Cytosine rich RNA (6) hairpin RNA (25) rRNA (11) tRNA-Arg2 (16) 23S rRNA (37) RNA (15) ssRNA (10) 8 (434) Splicing factor U2AF (172) VSV nucleocapsid (422) Pseudouridine synthase RluA (217) RNase II (664) Exon junction complex (410+146+89+1 50) S. solfataricus exosome (277+250) Serine protease subunit NS3 (451) Poly(rC)binding protein 2 (73) S.cerevisiae poly(A) polymerase (525) Rotavirus polymerase VP1 (1095) Exonuclease Rrp44 (760) Mtr4 (1010) [115] 2G4B [116] 2GIC [117] [118] 2I82 2IX1 [119] 2J0S [120] 2JEA [121] 2JLU [122] 2PY9 [123] 2Q66 [124] 2R7R [125] [126] 2VNU 2XGJ [127] 2XNR [128] 2XS2 [129] 2XZO Nab3-RRM (97) Murine Dazl (102) Upf1 helicase (623) [130] 3AEV Dim2p (219) [131] 3BX2 PUF4 (335) Polypyrimi dine (7) viral genomic RNA (45) 2.5 A B 1162 543 619 20 5 54 39 32 22 45 43 6 1 0.69 5 2.9 A R 1999 985 1014 36 11 55 36 16 19 32 49 10 11 0.57 3 tRNA-Phe (21) polyA (13) 2.1 2.7 A A E B 3019 4161 1453 1935 1565 2227 44 82 14 13 53 61 35 40 33 23 36 32 56 42 68 60 29 20 15 5 0.62 0.69 3 8 mRNA (15) 2.2 ACD T E 1436 591 845 30 6 61 25 46 38 38 46 21 9 0.75 19 substrate RNA (35) 2.3 AB C 1533 693 840 30 5 53 37 19 24 34 42 7 7 0.56 13 ssRNA (12) human telomeric RNA (12) 2.0 A C 1926 846 1079 40 7 61 34 29 35 41 50 19 9 0.68 11 2.6 B E 1061 513 548 19 7 55 33 34 39 37 41 9 0 0.72 3 polyA (5) 1.8 A X 1811 815 996 39 4 64 39 19 21 45 49 12 1 0.68 12 RNA (7) 2.6 A X 1955 906 1049 41 7 62 34 20 25 35 51 16 3 0.60 28 ssRNA (10) polyA (5) UCUU recognition sequence (12) 3'-UTRs of mRNA (8) 2.3 2.9 D A B C 3166 1389 1454 641 1712 748 66 30 10 5 53 62 37 30 33 25 37 23 44 34 62 49 22 10 9 0 0.69 0.68 10 31 1.6 A C 926 404 522 16 5 70 39 38 24 41 37 8 1 0.79 2 1.4 A B 1298 606 692 23 6 57 35 33 25 45 50 9 3 0.76 3 polyU (7) P. horikoshii 16S rRNA fragment (11) 3' UTR binding 2.4 A D 2006 937 1069 43 7 66 27 32 37 39 56 20 0 0.70 14 2.8 B C 2416 1132 1285 40 11 62 36 35 31 42 45 21 4 0.70 3 2.8 A C 2467 1098 1370 43 9 46 41 40 39 38 44 19 1 0.68 4 9 [132] [133] 3D2S 3I5X [134] [135] 3IEV 3K5Q [136] 3MDG [137] 3NMR [138] [139] 3O8C 3PF4 NA 3QJJ [140] 3R2C [141] 3RC8 [142] 3T5N [143] 4E78 [144] [145] 4H5P 4HOR [146] [147] 4J1G 4J7M [148] 4M59 [149] 4MDX [150] 4N2Q MBNL1 ZnF3/4 (70) Mss116p (563) GTPase era (308) FBF (412) CFI(m)25 (227+227) CUG-binding protein 1 (175) HCV NS3 helicase (666) CspB (67+67) RAMP Protein (243) NusB-NusE (148+83) Helicase SUPV3L1 (677) Lassa virus nucleoprotein (354) HCV polymerase (572) Nucleocapsid (245+245) IFIT (482) Nucleocapsid (235+235+235+ 235) Dom3Z (378) Chloroplast ppr10 (718+718) mRNA interferase MazF (117+117) Thylakoid assembly 8 (258) sequence (9) pre-mRNA (6) polyU (10) 16S rRNA (12) mRNA (9) pre-mRNA (6) UGU-rich mRNA (12) 1.7 1.9 A A E B 569 2228 273 969 296 1259 12 44 3 10 34 62 32 33 27 44 21 32 26 42 28 43 7 24 1 9 0.81 0.72 7 10 1.9 2.2 A A D B 2273 2597 1014 1177 1260 1420 38 40 9 9 65 52 39 40 47 32 38 32 51 41 51 46 19 21 2 2 0.77 0.62 5 5 2.2 AB C 1069 503 566 23 6 66 40 27 38 37 48 6 0 0.76 17 1.9 A B 1097 489 608 21 6 66 33 32 30 36 36 5 2 0.83 5 polyU (6) ssRNA (7) CRISPR Repeat RNA (12) BoxA RNA (12) RNA fragment (6) 2.0 1.4 A B C R 1909 893 909 419 1000 474 36 16 6 5 54 72 33 40 29 40 34 28 41 42 56 37 13 4 8 0 0.74 0.81 14 3 2.8 A Q 3191 1490 1701 52 12 53 32 44 40 50 63 27 9 0.65 3 1.9 AJ R 2273 1029 1243 37 9 62 35 50 35 54 54 23 1 0.78 4 2.9 A E 1471 668 802 32 6 65 31 34 31 37 49 10 1 0.63 19 ssRNA (6) RNA primertemplate pair (6+6) 1.8 A C 1910 857 1053 38 6 50 35 38 33 51 59 22 6 0.68 6 2.9 A PT 2100 1006 1095 46 10 53 38 17 26 34 50 13 7 0.51 9 polyU (14) polyC (5) 2.2 1.9 AB A E X 4483 1748 2173 765 2310 983 76 45 14 4 65 46 29 22 26 28 31 31 52 50 68 53 21 14 24 6 0.67 0.59 4 11 polyU (45) polyU (5) 2.8 1.7 C A E1934 B 3039 1268 1488 589 1550 679 47 29 14 5 60 46 33 26 19 24 33 27 42 40 60 42 13 9 12 8 0.56 0.60 1 13 psaJ RNA (18+18) 2.5 AB CD 7843 3665 4178 157 31 64 36 32 33 39 54 31 19 0.60 9 1.5 AB C 2127 958 1169 41 8 64 37 42 40 48 47 19 2 0.75 4 2.8 A B 814 375 439 10 5 60 28 31 33 40 39 4 6 0.70 10 mRNA (9) Zm4 13mer RNA (13) 10 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 19. Ruff, M., et al., Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science, 1991. 252(5013): p. 1682-9. Nissen, P., et al., The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Structure, 1999. 7(2): p. 143-56. Eiler, S., et al., Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step. EMBO J, 1999. 18(22): p. 6532-41. Delagoutte, B., D. Moras, and J. Cavarelli, tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding. EMBO J, 2000. 19(21): p. 5599-610. Silvian, L.F., J. Wang, and T.A. Steitz, Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin. Science, 1999. 285(5430): p. 1074-7. Fukai, S., et al., Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyltRNA synthetase. Cell, 2000. 103(5): p. 793-803. Yaremchuk, A., et al., Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J, 2002. 21(14): p. 3829-40. Yaremchuk, A., et al., A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyltRNA synthetase: comparison with histidyl-tRNA synthetase. J Mol Biol, 2001. 309(4): p. 989-1002. Kobayashi, T., et al., Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion. Nat Struct Biol, 2003. 10(6): p. 425-32. Sekine, S., et al., ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding. EMBO J, 2003. 22(3): p. 676-88. Sankaranarayanan, R., et al., The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell, 1999. 97(3): p. 371-81. Rath, V.L., et al., How glutaminyl-tRNA synthetase selects glutamine. Structure, 1998. 6(4): p. 439-49. Biou, V., et al., The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser). Science, 1994. 263(5152): p. 1404-10. Hauenstein, S., et al., Shape-selective RNA recognition by cysteinyl-tRNA synthetase. Nat Struct Mol Biol, 2004. 11(11): p. 1134-41. Tomita, K., et al., Structural basis for template-independent RNA polymerization. Nature, 2004. 430(7000): p. 700-4. Yang, X.L., et al., Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis. EMBO J, 2006. 25(12): p. 2919-29. Nakanishi, K., et al., Structural basis for anticodon recognition by methionyl-tRNA synthetase. Nat Struct Mol Biol, 2005. 12(10): p. 931-2. Tsunoda, M., et al., Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms. Nucleic Acids Res, 2007. 35(13): p. 4289-300. Tomita, K., et al., Complete crystallographic analysis of the dynamics of CCA sequence addition. Nature, 2006. 443(7114): p. 956-60. 11 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 31. 32. 33. 34. 35. 36. 37. 38. 39. Fukunaga, R. and S. Yokoyama, Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea. Nat Struct Mol Biol, 2007. 14(4): p. 272-9. Li de la Sierra-Gallay, I., et al., Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA. Nat Struct Mol Biol, 2006. 13(4): p. 376-7. Schmitt, E., et al., Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet. EMBO J, 1998. 17(23): p. 6819-26. Chimnaronk, S., et al., Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon. Biochemistry, 2009. 48(23): p. 505765. Konno, M., et al., Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP). FEBS J, 2009. 276(17): p. 4763-79. Goto-Ito, S., et al., Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation. Nat Struct Mol Biol, 2009. 16(10): p. 1109-15. Chiba, S., et al., Structural basis for the major role of O-phosphoseryl-tRNA kinase in the UGA-specific encoding of selenocysteine. Mol Cell, 2010. 39(3): p. 410-20. Osawa, T., et al., Structural basis of tRNA agmatinylation essential for AUA codon decoding. Nat Struct Mol Biol, 2011. 18(11): p. 1275-80. Zhou, C. and R.H. Huang, Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: insight into tRNA recognition and reaction mechanism. Proc Natl Acad Sci U S A, 2008. 105(42): p. 16142-7. Palioura, S., et al., The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation. Science, 2009. 325(5938): p. 321-5. Ito, K., et al., Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase. Nucleic Acids Res, 2012. 40(20): p. 10521-31. Hernandez, V., et al., Discovery of a novel class of boron-based antibacterials with activity against gram-negative bacteria. Antimicrob Agents Chemother, 2013. 57(3): p. 1394-403. Lu, M. and T.A. Steitz, Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-A resolution. Proc Natl Acad Sci U S A, 2000. 97(5): p. 2023-8. Fedorov, R., et al., Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins. Acta Crystallogr D Biol Crystallogr, 2001. 57(Pt 7): p. 968-76. Agalarov, S.C., et al., Structure of the S15,S6,S18-rRNA complex: assembly of the 30S ribosome central domain. Science, 2000. 288(5463): p. 107-13. Tishchenko, S., et al., Detailed analysis of RNA-protein interactions within the ribosomal protein S8-rRNA complex from the archaeon Methanococcus jannaschii. J Mol Biol, 2001. 311(2): p. 311-24. Perederina, A., et al., Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex. RNA, 2002. 8(12): p. 1548-57. Wimberly, B.T., et al., A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell, 1999. 97(4): p. 491-502. Nikulin, A., et al., Structure of the L1 protuberance in the ribosome. Nat Struct Biol, 2003. 10(2): p. 104-8. Merianos, H.J., J. Wang, and P.B. Moore, The structure of a ribosomal protein S8/spc operon mRNA complex. RNA, 2004. 10(6): p. 954-64. 12 40. 41. 42. 43. 44. 45. 46. 47. 48. 49. 50. 51. 52. 53. 54. 55. 56. 57. 58. Hamma, T. and A.R. Ferre-D'Amare, Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 A resolution. Structure, 2004. 12(5): p. 893-903. Tishchenko, S., et al., Structure of the ribosomal protein L1-mRNA complex at 2.1 A resolution: common features of crystal packing of L1-RNA complexes. Acta Crystallogr D Biol Crystallogr, 2006. 62(Pt 12): p. 1545-54. Ryter, J.M. and S.C. Schultz, Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA. EMBO J, 1998. 17(24): p. 7505-13. Batey, R.T., M.B. Sagar, and J.A. Doudna, Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle. J Mol Biol, 2001. 307(1): p. 229-46. Yin, Y.W. and T.A. Steitz, Structural Basis for the Transition from Initiation to Elongation Transcription in T7 RNA Polymerase. Science, 2002. 298(5597): p. 1387-1395. Tao, Y., et al., RNA synthesis in a cage--structural studies of reovirus polymerase lambda3. Cell, 2002. 111(5): p. 733-45. Huang, D.B., et al., Crystal structure of NF-kappaB (p50)2 complexed to a high-affinity RNA aptamer. Proc Natl Acad Sci U S A, 2003. 100(16): p. 9268-73. Xie, W., X. Liu, and R.H. Huang, Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate. Nat Struct Biol, 2003. 10(10): p. 781-8. Pan, H., et al., Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. Proc Natl Acad Sci U S A, 2003. 100(22): p. 12648-53. Ye, K., L. Malinina, and D.J. Patel, Recognition of small interfering RNA by a viral suppressor of RNA silencing. Nature, 2003. 426(6968): p. 874-8. Ma, J.B., K. Ye, and D.J. Patel, Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain. Nature, 2004. 429(6989): p. 318-22. Ferrer-Orta, C., et al., Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA. J Biol Chem, 2004. 279(45): p. 47212-21. Stein, A.J., et al., Structural insights into RNA quality control: the Ro autoantigen binds misfolded RNAs via its central cavity. Cell, 2005. 121(4): p. 529-39. Nowotny, M., et al., Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis. Cell, 2005. 121(7): p. 1005-16. Chao, J.A., et al., Dual modes of RNA-silencing suppression by Flock House virus protein B2. Nat Struct Mol Biol, 2005. 12(11): p. 952-7. Parker, J.S., S.M. Roe, and D. Barford, Structural insights into mRNA recognition from a PIWI domain-siRNA guide complex. Nature, 2005. 434(7033): p. 663-6. Gan, J., et al., Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell, 2006. 124(2): p. 355-66. Yuan, Y.R., et al., A potential protein-RNA recognition event along the RISC-loading pathway from the structure of A. aeolicus Argonaute with externally bound siRNA. Structure, 2006. 14(10): p. 1557-65. Xue, S., K. Calvin, and H. Li, RNA recognition and cleavage by a splicing endonuclease. Science, 2006. 312(5775): p. 906-10. 13 59. 60. 61. 62. 63. 64. 65. 66. 67. 68. 69. 70. 71. 72. 73. 74. 75. 76. 77. 78. 79. 80. Placido, D., et al., A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1. Structure, 2007. 15(4): p. 395404. Liu, S., et al., Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP. Science, 2007. 316(5821): p. 115-20. Soler, N., D. Fourmy, and S. Yoshizawa, Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB. J Mol Biol, 2007. 370(4): p. 728-41. Chao, J.A., et al., Structural basis for the coevolution of a viral RNA-protein complex. Nat Struct Mol Biol, 2008. 15(1): p. 103-5. Ye, J.D., et al., Synthetic antibodies for specific recognition and crystallization of structured RNA. Proc Natl Acad Sci U S A, 2008. 105(1): p. 82-7. Blower, T.R., et al., A processed noncoding RNA regulates an altruistic bacterial antiviral system. Nat Struct Mol Biol, 2011. 18(2): p. 185-90. Sashital, D.G., M. Jinek, and J.A. Doudna, An RNA-induced conformational change required for CRISPR RNA cleavage by the endoribonuclease Cse3. Nat Struct Mol Biol, 2011. 18(6): p. 680-7. Luo, D., et al., Structural insights into RNA recognition by RIG-I. Cell, 2011. 147(2): p. 409-22. Chen, H.Y., et al., Structural basis for RNA-silencing suppression by Tomato aspermy virus protein 2b. EMBO Rep, 2008. 9(8): p. 754-60. Cheng, A., S.M. Wong, and Y.A. Yuan, Structural basis for dsRNA recognition by NS1 protein of influenza A virus. Cell Res, 2009. 19(2): p. 187-95. Okada, C., et al., A high-resolution structure of the pre-microRNA nuclear export machinery. Science, 2009. 326(5957): p. 1275-9. Zamyatkin, D.F., et al., Structural insights into mechanisms of catalysis and inhibition in Norwalk virus polymerase. J Biol Chem, 2008. 283(12): p. 7705-12. Alian, A., et al., Structure of a TrmA-RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases. Proc Natl Acad Sci U S A, 2008. 105(19): p. 6876-81. Long, S.B., et al., Crystal structure of an RNA aptamer bound to thrombin. RNA, 2008. 14(12): p. 2504-12. Alian, A., et al., Crystal structure of an RluF-RNA complex: a base-pair rearrangement is the key to selectivity of RluF for U2604 of the ribosome. J Mol Biol, 2009. 388(4): p. 785-800. Li, X., et al., The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA. J Biol Chem, 2009. 284(20): p. 13881-91. Tu, C., et al., Structural basis for binding of RNA and cofactor by a KsgA methyltransferase. Structure, 2009. 17(3): p. 374-85. Perederina, A., et al., Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domain. EMBO J, 2010. 29(4): p. 761-9. Kimberlin, C.R., et al., Ebolavirus VP35 uses a bimodal strategy to bind dsRNA for innate immune suppression. Proc Natl Acad Sci U S A, 2010. 107(1): p. 314-9. Hardin, J.W., Y.X. Hu, and D.B. McKay, Structure of the RNA binding domain of a DEAD-box helicase bound to its ribosomal RNA target reveals a novel mode of recognition by an RNA recognition motif. J Mol Biol, 2010. 402(2): p. 412-27. Tian, Y., et al., Structural basis for piRNA 2'-O-methylated 3'-end recognition by Piwi PAZ (Piwi/Argonaute/Zwille) domains. Proc Natl Acad Sci U S A, 2011. 108(3): p. 903-10. Thomas, S.R., et al., Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis. Nucleic Acids Res, 2011. 39(6): p. 2445-57. 14 81. 82. 83. 84. 85. 86. 87. 88. 89. 90. 91. 92. 93. 94. 95. 96. 97. 98. 99. Gong, P. and O.B. Peersen, Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase. Proc Natl Acad Sci U S A, 2010. 107(52): p. 22505-10. Teplova, M., et al., Structure-function studies of nucleocytoplasmic transport of retroviral genomic RNA by mRNA export factor TAP. Nat Struct Mol Biol, 2011. 18(9): p. 990-8. Walden, W.E., et al., Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. Science, 2006. 314(5807): p. 1903-8. Parizotto, E.A., E.D. Lowe, and J.S. Parker, Structural basis for duplex RNA recognition and cleavage by Archaeoglobus fulgidus C3PO. Nat Struct Mol Biol, 2013. 20(3): p. 380-6. Short, F.L., et al., Selectivity and self-assembly in the control of a bacterial toxin by an antitoxic noncoding RNA pseudoknot. Proc Natl Acad Sci U S A, 2013. 110(3): p. E241-9. Singh, M., et al., Structural basis for telomerase RNA recognition and RNP assembly by the holoenzyme La family protein p65. Mol Cell, 2012. 47(1): p. 16-26. Hastie, K.M., et al., Structural basis for the dsRNA specificity of the Lassa virus NP exonuclease. PLoS One, 2012. 7(8): p. e44211. Donovan, J., M. Dufner, and A. Korennykh, Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1. Proc Natl Acad Sci U S A, 2013. 110(5): p. 1652-7. Shao, Y. and H. Li, Recognition and cleavage of a nonstructured CRISPR RNA by its processing endoribonuclease Cas6. Structure, 2013. 21(3): p. 38593. Rumnieks, J. and K. Tars, Crystal structure of the bacteriophage Qbeta coat protein in complex with the RNA operator of the replicase gene. J Mol Biol, 2014. 426(5): p. 1039-49. Hodel, A.E., P.D. Gershon, and F.A. Quiocho, Structural basis for sequence-nonspecific recognition of 5'-capped mRNA by a cap-modifying enzyme. Mol Cell, 1998. 1(3): p. 443-7. Antson, A.A., et al., Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA. Nature, 1999. 401(6750): p. 235-42. Deo, R.C., et al., Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell, 1999. 98(6): p. 835-45. Wang, X. and T.M. Tanaka Hall, Structural basis for recognition of AU-rich element RNA by the HuD protein. Nat Struct Biol, 2001. 8(2): p. 141-5. Yang, X., et al., Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping. Nat Struct Biol, 2001. 8(11): p. 968-73. Wild, K., I. Sinning, and S. Cusack, Crystal structure of an early protein-RNA assembly complex of the signal recognition particle. Science, 2001. 294(5542): p. 598-601. Hoang, C. and A.R. Ferre-D'Amare, Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme. Cell, 2001. 107(7): p. 929-39. Deo, R.C., et al., Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer. Cell, 2002. 108(1): p. 71-81. Schumacher, M.A., et al., Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J, 2002. 21(13): p. 3546-56. 15 100. 101. 102. 103. 104. 105. 106. 107. 108. 109. 110. 111. 112. 113. 114. 115. 116. 117. 118. 119. 120. 121. Hainzl, T., S. Huang, and A.E. Sauer-Eriksson, Structure of the SRP19 RNA complex and implications for signal recognition particle assembly. Nature, 2002. 417(6890): p. 767-71. Rupert, P.B., et al., Transition state stabilization by a catalytic RNA. Science, 2002. 298(5597): p. 1421-4. Thore, S., et al., Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. Common features of RNA binding in archaea and eukarya. J Biol Chem, 2003. 278(2): p. 1239-47. Wang, X., et al., Modular recognition of RNA by a human pumilio-homology domain. Cell, 2002. 110(4): p. 501-12. Salgado, P.S., et al., The structural basis for RNA specificity and Ca2+ inhibition of an RNA-dependent RNA polymerase. Structure, 2004. 12(2): p. 307-16. Kumarevel, T., H. Mizuno, and P.K.R. Kumar, Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand. Nature, 2005. 434(7030): p. 183-191. Yoshizawa, S., et al., Structural basis for mRNA recognition by elongation factor SelB. Nat Struct Mol Biol, 2005. 12(2): p. 198-203. Teplova, M., et al., Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen. Mol Cell, 2006. 21(1): p. 75-85. Bogden, C.E., et al., The structural basis for terminator recognition by the Rho transcription termination factor. Mol Cell, 1999. 3(4): p. 487-93. Teplova, M., et al., Protein-RNA and protein-protein recognition by dual KH1/2 domains of the neuronal splicing factor Nova-1. Structure, 2011. 19(7): p. 930-44. Beuth, B., et al., Structure of a Mycobacterium tuberculosis NusA-RNA complex. EMBO J, 2005. 24(20): p. 3576-87. Losey, H.C., A.J. Ruthenburg, and G.L. Verdine, Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA. Nat Struct Mol Biol, 2006. 13(2): p. 153-9. Lee, T.T., S. Agarwalla, and R.M. Stroud, A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function. Cell, 2005. 120(5): p. 599-611. Callaghan, A.J., et al., Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Nature, 2005. 437(7062): p. 1187-91. Sengoku, T., et al., Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell, 2006. 125(2): p. 287-300. Sickmier, E.A., et al., Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65. Mol Cell, 2006. 23(1): p. 49-59. Green, T.J., et al., Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science, 2006. 313(5785): p. 357-60. Hoang, C., et al., Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure. Mol Cell, 2006. 24(4): p. 535-45. Frazao, C., et al., Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex. Nature, 2006. 443(7107): p. 110-4. Bono, F., et al., The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell, 2006. 126(4): p. 713-25. Lorentzen, E., et al., RNA channelling by the archaeal exosome. EMBO Rep, 2007. 8(5): p. 470-6. Luo, D., et al., Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein. EMBO J, 2008. 27(23): p. 3209-19. 16 122. 123. 124. 125. 126. 127. 128. 129. 130. 131. 132. 133. 134. 135. 136. 137. 138. 139. Du, Z., et al., X-ray crystallographic and NMR studies of protein-protein and protein-nucleic acid interactions involving the KH domains from human poly(C)-binding protein-2. RNA, 2007. 13(7): p. 1043-51. Balbo, P.B. and A. Bohm, Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis. Structure, 2007. 15(9): p. 1117-31. Lu, X., et al., Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase VP1. Structure, 2008. 16(11): p. 1678-88. Lorentzen, E., et al., Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell, 2008. 29(6): p. 717-28. Weir, J.R., et al., Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance. Proc Natl Acad Sci U S A, 2010. 107(27): p. 12139-44. Lunde, B.M., M. Horner, and A. Meinhart, Structural insights into cis element recognition of non-polyadenylated RNAs by the Nab3-RRM. Nucleic Acids Res, 2011. 39(1): p. 337-46. Jenkins, H.T., B. Malkova, and T.A. Edwards, Kinked beta-strands mediate high-affinity recognition of mRNA targets by the germ-cell regulator DAZL. Proc Natl Acad Sci U S A, 2011. 108(45): p. 18266-71. Chakrabarti, S., et al., Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2. Mol Cell, 2011. 41(6): p. 693-703. Jia, M.Z., et al., An archaeal Dim2-like protein, aDim2p, forms a ternary complex with a/eIF2 alpha and the 3' end fragment of 16S rRNA. J Mol Biol, 2010. 398(5): p. 774-85. Miller, M.T., J.J. Higgin, and T.M. Hall, Basis of altered RNA-binding specificity by PUF proteins revealed by crystal structures of yeast Puf4p. Nat Struct Mol Biol, 2008. 15(4): p. 397-402. Teplova, M. and D.J. Patel, Structural insights into RNA recognition by the alternative-splicing regulator muscleblind-like MBNL1. Nat Struct Mol Biol, 2008. 15(12): p. 1343-51. Del Campo, M. and A.M. Lambowitz, Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol Cell, 2009. 35(5): p. 598-609. Tu, C., et al., Structure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis. Proc Natl Acad Sci U S A, 2009. 106(35): p. 14843-8. Wang, Y., et al., Structural basis for specific recognition of multiple mRNA targets by a PUF regulatory protein. Proc Natl Acad Sci U S A, 2009. 106(48): p. 20186-91. Yang, Q., G.M. Gilmartin, and S. Doublie, Structural basis of UGUA recognition by the Nudix protein CFI(m)25 and implications for a regulatory role in mRNA 3' processing. Proc Natl Acad Sci U S A, 2010. 107(22): p. 10062-7. Teplova, M., et al., Structural insights into RNA recognition by the alternate-splicing regulator CUG-binding protein 1. Structure, 2010. 18(10): p. 1364-77. Appleby, T.C., et al., Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV. J Mol Biol, 2011. 405(5): p. 1139-53. Sachs, R., et al., RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solution. RNA, 2012. 18(1): p. 65-76. 17 140. 141. 142. 143. 144. 145. 146. 147. 148. 149. 150. Stagno, J.R., et al., Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination. Nucleic Acids Res, 2011. 39(17): p. 7803-15. Jedrzejczak, R., et al., Human Suv3 protein reveals unique features among SF2 helicases. Acta Crystallogr D Biol Crystallogr, 2011. 67(Pt 11): p. 98896. Hastie, K.M., et al., Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding. Proc Natl Acad Sci U S A, 2011. 108(48): p. 19365-70. Mosley, R.T., et al., Structure of hepatitis C virus polymerase in complex with primer-template RNA. J Virol, 2012. 86(12): p. 6503-11. Raymond, D.D., et al., Phleboviruses encapsidate their genomes by sequestering RNA bases. Proc Natl Acad Sci U S A, 2012. 109(47): p. 19208-13. Abbas, Y.M., et al., Structural basis for viral 5'-PPP-RNA recognition by human IFIT proteins. Nature, 2013. 494(7435): p. 60-4. Niu, F., et al., Structure of the Leanyer orthobunyavirus nucleoprotein-RNA complex reveals unique architecture for RNA encapsidation. Proc Natl Acad Sci U S A, 2013. 110(22): p. 9054-9. Jiao, X., et al., A mammalian pre-mRNA 5' end capping quality control mechanism and an unexpected link of capping to pre-mRNA processing. Mol Cell, 2013. 50(1): p. 104-15. Yin, P., et al., Structural basis for the modular recognition of single-stranded RNA by PPR proteins. Nature, 2013. 504(7478): p. 168-71. Simanshu, D.K., et al., Structural basis of mRNA recognition and cleavage by toxin MazF and its regulation by antitoxin MazE in Bacillus subtilis. Mol Cell, 2013. 52(3): p. 447-58. Ke, J., et al., Structural basis for RNA recognition by a dimeric PPR-protein complex. Nat Struct Mol Biol, 2013. 20(12): p. 1377-82. 18