4V7D

Structure of the Ribosome with Elongation Factor G Trapped in the Pre-Translocation State (pre-translocation 70S*tRNA*EF-G structure)

これはPDB形式変換不可エントリーです。

4V7D の概要

• エントリーDOI: 10.2210/pdb4v7d/pdb
• 関連するPDBエントリー: 3J5T 3J5U
• EMDBエントリー: 5799 5800
• 関連するBIRD辞書のPRD_ID: PRD_000226
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L10, 50S ribosomal protein L11, ... (60 entities in total)
• 機能のキーワード: translation, ef-g, single particle analysis, pre-translocation translation complex, viomycin, translation-antibiotic complex, translation/antibiotic
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 60
• 化学式量合計: 2330687.26

構造登録者

Brilot, A.F.,Korostelev, A.A.,Ermolenko, D.N.,Grigorieff, N. (登録日: 2013-11-21, 公開日: 2014-07-09, 最終更新日: 2025-03-26)

主引用文献

Brilot, A.F.,Korostelev, A.A.,Ermolenko, D.N.,Grigorieff, N.
Structure of the ribosome with elongation factor G trapped in the pretranslocation state.
Proc.Natl.Acad.Sci.USA, 110:20994-20999, 2013

PubMed Abstract: During protein synthesis, tRNAs and their associated mRNA codons move sequentially on the ribosome from the A (aminoacyl) site to the P (peptidyl) site to the E (exit) site in a process catalyzed by a universally conserved ribosome-dependent GTPase [elongation factor G (EF-G) in prokaryotes and elongation factor 2 (EF-2) in eukaryotes]. Although the high-resolution structure of EF-G bound to the posttranslocation ribosome has been determined, the pretranslocation conformation of the ribosome bound with EF-G and A-site tRNA has evaded visualization owing to the transient nature of this state. Here we use electron cryomicroscopy to determine the structure of the 70S ribosome with EF-G, which is trapped in the pretranslocation state using antibiotic viomycin. Comparison with the posttranslocation ribosome shows that the small subunit of the pretranslocation ribosome is rotated by ∼12° relative to the large subunit. Domain IV of EF-G is positioned in the cleft between the body and head of the small subunit outwardly of the A site and contacts the A-site tRNA. Our findings suggest a model in which domain IV of EF-G promotes the translocation of tRNA from the A to the P site as the small ribosome subunit spontaneously rotates back from the hybrid, rotated state into the nonrotated posttranslocation state.

PubMed: 24324137
DOI: 10.1073/pnas.1311423110

実験手法

ELECTRON MICROSCOPY (7.6 Å)