5UYQ

70S ribosome bound with near-cognate ternary complex base-paired to A site codon, closed 30S (Structure III-nc)

これはPDB形式変換不可エントリーです。

5UYQ の概要

• エントリーDOI: 10.2210/pdb5uyq/pdb
• 関連するPDBエントリー: 5UYK 5UYL 5UYM 5UYN 5UYP
• EMDBエントリー: 8615 8616 8617 8618 8619 8620
• 分子名称: 50S ribosomal protein L2, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (63 entities in total)
• 機能のキーワード: ribosome, ef-tu, trna
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 60
• 化学式量合計: 2288496.04

構造登録者

Loveland, A.B.,Demo, G.,Grigorieff, N.,Korostelev, A.A. (登録日: 2017-02-24, 公開日: 2017-06-07, 最終更新日: 2024-03-13)

主引用文献

Loveland, A.B.,Demo, G.,Grigorieff, N.,Korostelev, A.A.
Ensemble cryo-EM elucidates the mechanism of translation fidelity
Nature, 546:113-117, 2017

PubMed Abstract: Gene translation depends on accurate decoding of mRNA, the structural mechanism of which remains poorly understood. Ribosomes decode mRNA codons by selecting cognate aminoacyl-tRNAs delivered by elongation factor Tu (EF-Tu). Here we present high-resolution structural ensembles of ribosomes with cognate or near-cognate aminoacyl-tRNAs delivered by EF-Tu. Both cognate and near-cognate tRNA anticodons explore the aminoacyl-tRNA-binding site (A site) of an open 30S subunit, while inactive EF-Tu is separated from the 50S subunit. A transient conformation of decoding-centre nucleotide G530 stabilizes the cognate codon-anticodon helix, initiating step-wise 'latching' of the decoding centre. The resulting closure of the 30S subunit docks EF-Tu at the sarcin-ricin loop of the 50S subunit, activating EF-Tu for GTP hydrolysis and enabling accommodation of the aminoacyl-tRNA. By contrast, near-cognate complexes fail to induce the G530 latch, thus favouring open 30S pre-accommodation intermediates with inactive EF-Tu. This work reveals long-sought structural differences between the pre-accommodation of cognate and near-cognate tRNAs that elucidate the mechanism of accurate decoding.

PubMed: 28538735
DOI: 10.1038/nature22397

実験手法

ELECTRON MICROSCOPY (3.8 Å)