7AS8

Bacillus subtilis ribosome quality control complex state B. Ribosomal 50S subunit with P-tRNA, RqcH, and RqcP/YabO

7AS8 の概要

• エントリーDOI: 10.2210/pdb7as8/pdb
• EMDBエントリー: 11889
• 分子名称: Rqc2 homolog RqcH, 50S ribosomal protein L6, 50S ribosomal protein L11, ... (33 entities in total)
• 機能のキーワード: 50s, trna, rqc, rqch, peptidyl-trna, translation, rqcp, yabo, alanine tailing
• 由来する生物種: Bacillus subtilis (strain 168); 詳細
• タンパク質・核酸の鎖数: 33
• 化学式量合計: 1460684.66

構造登録者

Crowe-McAuliffe, C.,Wilson, D.N. (登録日: 2020-10-27, 公開日: 2020-12-09, 最終更新日: 2024-10-16)

主引用文献

Crowe-McAuliffe, C.,Takada, H.,Murina, V.,Polte, C.,Kasvandik, S.,Tenson, T.,Ignatova, Z.,Atkinson, G.C.,Wilson, D.N.,Hauryliuk, V.
Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP.
Mol.Cell, 81:115-, 2021

PubMed Abstract: In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, leaving an unfinished polypeptide still attached to the large subunit. Ancient and conserved NEMF family RQC proteins target these incomplete proteins for degradation by the addition of C-terminal "tails." How such tailing can occur without the regular suite of translational components is, however, unclear. Using single-particle cryo-electron microscopy (EM) of native complexes, we show that C-terminal tailing in Bacillus subtilis is mediated by NEMF protein RqcH in concert with RqcP, an Hsp15 family protein. Our structures reveal how these factors mediate tRNA movement across the ribosomal 50S subunit to synthesize polypeptides in the absence of mRNA or the small subunit.

PubMed: 33259810
DOI: 10.1016/j.molcel.2020.11.002

実験手法

ELECTRON MICROSCOPY (2.9 Å)