7ST7

Pre translocation intermediate stalled with viomycin and bound with EF-G in a GDP and Pi state (Structure III-vio)

これはPDB形式変換不可エントリーです。

7ST7 の概要

• エントリーDOI: 10.2210/pdb7st7/pdb
• EMDBエントリー: 25420 25421
• 関連するBIRD辞書のPRD_ID: PRD_000226
• 分子名称: 23S rRNA, 50S ribosomal protein L11, 50S ribosomal protein L13, ... (61 entities in total)
• 機能のキーワード: ribosome-antibiotic complex, ef-g, viomycin, gtp, ribosome/antibiotic
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 59
• 化学式量合計: 2284080.03

構造登録者

Carbone, C.E.,Korostelev, A.A. (登録日: 2021-11-12, 公開日: 2022-02-23)

主引用文献

Carbone, C.E.,Loveland, A.B.,Gamper Jr., H.B.,Hou, Y.M.,Demo, G.,Korostelev, A.A.
Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP.
Nat Commun, 12:7236-7236, 2021

PubMed Abstract: During translation, a conserved GTPase elongation factor-EF-G in bacteria or eEF2 in eukaryotes-translocates tRNA and mRNA through the ribosome. EF-G has been proposed to act as a flexible motor that propels tRNA and mRNA movement, as a rigid pawl that biases unidirectional translocation resulting from ribosome rearrangements, or by various combinations of motor- and pawl-like mechanisms. Using time-resolved cryo-EM, we visualized GTP-catalyzed translocation without inhibitors, capturing elusive structures of ribosome•EF-G intermediates at near-atomic resolution. Prior to translocation, EF-G binds near peptidyl-tRNA, while the rotated 30S subunit stabilizes the EF-G GTPase center. Reverse 30S rotation releases Pi and translocates peptidyl-tRNA and EF-G by ~20 Å. An additional 4-Å translocation initiates EF-G dissociation from a transient ribosome state with highly swiveled 30S head. The structures visualize how nearly rigid EF-G rectifies inherent and spontaneous ribosomal dynamics into tRNA-mRNA translocation, whereas GTP hydrolysis and Pi release drive EF-G dissociation.

PubMed: 34903725
DOI: 10.1038/s41467-021-27415-0

実験手法

ELECTRON MICROSCOPY (3.2 Å)