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PDBsum entry 3cme
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Contents |
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237 a.a.
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337 a.a.
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246 a.a.
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140 a.a.
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172 a.a.
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119 a.a.
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29 a.a.
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160 a.a.
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70 a.a.
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142 a.a.
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132 a.a.
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145 a.a.
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194 a.a.
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186 a.a.
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115 a.a.
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143 a.a.
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95 a.a.
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150 a.a.
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81 a.a.
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119 a.a.
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53 a.a.
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65 a.a.
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154 a.a.
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82 a.a.
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142 a.a.
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73 a.a.
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56 a.a.
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46 a.a.
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92 a.a.
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_SR
×108
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_NA
×75
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_CL
×22
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_MG
×93
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_CD
×5
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__K
×2
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* Residue conservation analysis
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PDB id:
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Ribosome
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Title:
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The structure of ca and cca-phe-cap-bio bound to the large ribosomal subunit of haloarcula marismortui
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Structure:
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50s ribosomal protein l2p. Chain: a. Synonym: hmal2, hl4. 50s ribosomal protein l3p. Chain: b. Synonym: hmal3, hl1. 50s ribosomal protein l4p. Chain: c. Synonym: hmal4, hl6.
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Source:
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Haloarcula marismortui. Halobacterium marismortui. Organism_taxid: 2238. Synthetic: yes. Synthetic construct. Organism_taxid: 32630. Organism_taxid: 32630
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Resolution:
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2.95Å
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R-factor:
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0.198
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R-free:
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0.255
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Authors:
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M.Simonovic,T.A.Steitz
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Key ref:
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M.Simonović
and
T.A.Steitz
(2008).
Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3'-hydroxyl group of A76 of the unacylated A-site tRNA.
Rna,
14,
2372-2378.
PubMed id:
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Date:
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21-Mar-08
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Release date:
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23-Sep-08
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PROCHECK
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Headers
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References
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P20276
(RL2_HALMA) -
Large ribosomal subunit protein uL2 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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240 a.a.
237 a.a.
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P20279
(RL3_HALMA) -
Large ribosomal subunit protein uL3 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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338 a.a.
337 a.a.
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P12735
(RL4_HALMA) -
Large ribosomal subunit protein uL4 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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246 a.a.
246 a.a.
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P14124
(RL5_HALMA) -
Large ribosomal subunit protein uL5 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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177 a.a.
140 a.a.
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P14135
(RL6_HALMA) -
Large ribosomal subunit protein uL6 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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178 a.a.
172 a.a.
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P12743
(RL7A_HALMA) -
Large ribosomal subunit protein eL8 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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120 a.a.
119 a.a.
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P15825
(RL10_HALMA) -
Large ribosomal subunit protein uL10 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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348 a.a.
29 a.a.*
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P60617
(RL10E_HALMA) -
Large ribosomal subunit protein uL16 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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177 a.a.
160 a.a.
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P14122
(RL11_HALMA) -
Large ribosomal subunit protein uL11 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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162 a.a.
70 a.a.
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P29198
(RL13_HALMA) -
Large ribosomal subunit protein uL13 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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145 a.a.
142 a.a.
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P22450
(RL14_HALMA) -
Large ribosomal subunit protein uL14 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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132 a.a.
132 a.a.
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P12737
(RL15_HALMA) -
Large ribosomal subunit protein uL15 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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165 a.a.
145 a.a.
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P60618
(RL15E_HALMA) -
Large ribosomal subunit protein eL15 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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196 a.a.
194 a.a.
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P14123
(RL18_HALMA) -
Large ribosomal subunit protein uL18 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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187 a.a.
186 a.a.
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P12733
(RL18E_HALMA) -
Large ribosomal subunit protein eL18 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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116 a.a.
115 a.a.
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P14119
(RL19E_HALMA) -
Large ribosomal subunit protein eL19 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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149 a.a.
143 a.a.
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P12734
(RL21_HALMA) -
Large ribosomal subunit protein eL21 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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96 a.a.
95 a.a.
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P10970
(RL22_HALMA) -
Large ribosomal subunit protein uL22 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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155 a.a.
150 a.a.
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P12732
(RL23_HALMA) -
Large ribosomal subunit protein uL23 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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85 a.a.
81 a.a.
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P10972
(RL24_HALMA) -
Large ribosomal subunit protein uL24 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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120 a.a.
119 a.a.
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P14116
(RL24E_HALMA) -
Large ribosomal subunit protein eL24 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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67 a.a.
53 a.a.
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P10971
(RL29_HALMA) -
Large ribosomal subunit protein uL29 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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71 a.a.
65 a.a.
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P14121
(RL30_HALMA) -
Large ribosomal subunit protein uL30 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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154 a.a.
154 a.a.
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P18138
(RL31_HALMA) -
Large ribosomal subunit protein eL31 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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92 a.a.
82 a.a.
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P12736
(RL32_HALMA) -
Large ribosomal subunit protein eL32 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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241 a.a.
142 a.a.
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P60619
(RL37A_HALMA) -
Large ribosomal subunit protein eL43 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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92 a.a.
73 a.a.
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P32410
(RL37_HALMA) -
Large ribosomal subunit protein eL37 from Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
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Seq: Struc:
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57 a.a.
56 a.a.
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Enzyme class:
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Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2, 3:
E.C.?
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Rna
14:2372-2378
(2008)
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PubMed id:
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Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3'-hydroxyl group of A76 of the unacylated A-site tRNA.
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M.Simonović,
T.A.Steitz.
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ABSTRACT
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The last step in ribosome-catalyzed protein synthesis is the hydrolytic release
of the newly formed polypeptide from the P-site bound tRNA. Hydrolysis of the
ester link of the peptidyl-tRNA is stimulated normally by the binding of release
factors (RFs). However, an unacylated tRNA or just CCA binding to the ribosomal
A site can also stimulate deacylation under some nonphysiological conditions.
Although the sequence of events is well described by biochemical studies, the
structural basis of the mechanism underlying this process is not well
understood. Two new structures of the large ribosomal subunit of Haloarcula
marismortui complexed with a peptidyl-tRNA analog in the P site and two
oligonucleotide mimics of unacylated tRNA, CCA and CA, in the A site show that
the binding of either CA or CCA induces a very similar conformational change in
the peptidyl-transferase center as induced by aminoacyl-CCA. However, only CCA
positions a water molecule appropriately to attack the carbonyl carbon of the
peptidyl-tRNA and stabilizes the proper orientation of the ester link for
hydrolysis. We, thus, conclude that both the ability of the O3'-hydroxyl group
of the A-site A76 to position the water and the A-site CCA induced
conformational change of the PTC are critical for the catalysis of the
deacylation of the peptidyl-tRNA by CCA, and perhaps, an analogous mechanism is
used by RFs.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.Meskauskas,
and
J.D.Dinman
(2010).
A molecular clamp ensures allosteric coordination of peptidyltransfer and ligand binding to the ribosomal A-site.
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Nucleic Acids Res,
38,
7800-7813.
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H.Betat,
C.Rammelt,
and
M.Mörl
(2010).
tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization.
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Cell Mol Life Sci,
67,
1447-1463.
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A.Yonath
(2009).
Large facilities and the evolving ribosome, the cellular machine for genetic-code translation.
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J R Soc Interface,
6,
S575-S585.
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M.Simonović,
and
T.A.Steitz
(2009).
A structural view on the mechanism of the ribosome-catalyzed peptide bond formation.
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Biochim Biophys Acta,
1789,
612-623.
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R.Egel
(2009).
Peptide-dominated membranes preceding the genetic takeover by RNA: latest thinking on a classic controversy.
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Bioessays,
31,
1100-1109.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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');
}
}
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