4V69

Ternary complex-bound E.coli 70S ribosome.

これはPDB形式変換不可エントリーです。

4V69 の概要

• エントリーDOI: 10.2210/pdb4v69/pdb
• 関連するPDBエントリー: 1ob2 2i2u 2i2v 2j00
• EMDBエントリー: 5036
• 分子名称: 30S ribosomal protein S10, 30S ribosomal protein S19, 30S ribosomal protein S20, ... (59 entities in total)
• 機能のキーワード: ribosome, ternary complex, flexible fitting, cryo-em, 30s, 50s, trna, mrna, ef-tu, 70s, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, antibiotic resistance, repressor, transcription, transcription regulation, transcription termination, translation regulation, trna-binding, methylation, endonuclease, hydrolase, nuclease, cell membrane, elongation factor, gtp-binding, membrane, nucleotide-binding, phosphoprotein, protein biosynthesis
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 58
• 化学式量合計: 2257224.11

構造登録者

Villa, E.,Sengupta, J.,Trabuco, L.G.,LeBarron, J.,Baxter, W.T.,Shaikh, T.R.,Grassucci, R.A.,Nissen, P.,Ehrenberg, M.,Schulten, K.,Frank, J. (登録日: 2008-12-11, 公開日: 2014-07-09, 最終更新日: 2024-02-28)

主引用文献

Villa, E.,Sengupta, J.,Trabuco, L.G.,LeBarron, J.,Baxter, W.T.,Shaikh, T.R.,Grassucci, R.A.,Nissen, P.,Ehrenberg, M.,Schulten, K.,Frank, J.
Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis
Proc.Natl.Acad.Sci.USA, 106:1063-1068, 2009

PubMed Abstract: In translation, elongation factor Tu (EF-Tu) molecules deliver aminoacyl-tRNAs to the mRNA-programmed ribosome. The GTPase activity of EF-Tu is triggered by ribosome-induced conformational changes of the factor that play a pivotal role in the selection of the cognate aminoacyl-tRNAs. We present a 6.7-A cryo-electron microscopy map of the aminoacyl-tRNA x EF-Tu x GDP x kirromycin-bound Escherichia coli ribosome, together with an atomic model of the complex obtained through molecular dynamics flexible fitting. The model reveals the conformational changes in the conserved GTPase switch regions of EF-Tu that trigger hydrolysis of GTP, along with key interactions, including those between the sarcin-ricin loop and the P loop of EF-Tu, and between the effector loop of EF-Tu and a conserved region of the 16S rRNA. Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism.

PubMed: 19122150
DOI: 10.1073/pnas.0811370106

実験手法

ELECTRON MICROSCOPY (6.7 Å)