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1R2X

Coordinates of L11 with 58nts of 23S rRNA fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome

1R2X の概要
エントリーDOI10.2210/pdb1r2x/pdb
関連するPDBエントリー1FFK 1QZA 1QZB 1QZC 1QZD 1R2W
EMDBエントリー1055
分子名称58nts of 23S rRNA, 50S ribosomal protein L11 (2 entities in total)
機能のキーワードrna, ribosomal protein, rna binding protein-rna complex, rna binding protein/rna
由来する生物種Thermotoga maritima
タンパク質・核酸の鎖数2
化学式量合計33802.99
構造登録者
Valle, M.,Zavialov, A.,Li, W.,Stagg, S.M.,Sengupta, J.,Nielsen, R.C.,Nissen, P.,Harvey, S.C.,Ehrenberg, M.,Frank, J. (登録日: 2003-09-30, 公開日: 2003-11-04, 最終更新日: 2024-02-14)
主引用文献Valle, M.,Zavialov, A.,Li, W.,Stagg, S.M.,Sengupta, J.,Nielsen, R.C.,Nissen, P.,Harvey, S.C.,Ehrenberg, M.,Frank, J.
Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron Microscopy
Nat.Struct.Biol., 10:899-906, 2003
Cited by
PubMed Abstract: Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of approximately 9 A, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome.
PubMed: 14566331
DOI: 10.1038/nsb1003
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (9 Å)
構造検証レポート
Validation report summary of 1r2x
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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