5NGM

2.9S structure of the 70S ribosome composing the S. aureus 100S complex

これはPDB形式変換不可エントリーです。

5NGM の概要

• エントリーDOI: 10.2210/pdb5ngm/pdb
• EMDBエントリー: 3637 3640
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (53 entities in total)
• 機能のキーワード: ribosome cryo-em structural biology hibernation, ribosome
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 52
• 化学式量合計: 2170506.34

構造登録者

Matzov, D.,Aibara, S.,Zimmerman, E.,Bashan, A.,Amunts, A.,Yonath, A. (登録日: 2017-03-18, 公開日: 2017-10-04, 最終更新日: 2024-11-06)

主引用文献

Matzov, D.,Aibara, S.,Basu, A.,Zimmerman, E.,Bashan, A.,Yap, M.F.,Amunts, A.,Yonath, A.E.
The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus.
Nat Commun, 8:723-723, 2017

PubMed Abstract: Formation of 100S ribosome dimer is generally associated with translation suppression in bacteria. Trans-acting factors ribosome modulation factor (RMF) and hibernating promoting factor (HPF) were shown to directly mediate this process in E. coli. Gram-positive S. aureus lacks an RMF homolog and the structural basis for its 100S formation was not known. Here we report the cryo-electron microscopy structure of the native 100S ribosome from S. aureus, revealing the molecular mechanism of its formation. The structure is distinct from previously reported analogs and relies on the HPF C-terminal extension forming the binding platform for the interactions between both of the small ribosomal subunits. The 100S dimer is formed through interactions between rRNA h26, h40, and protein uS2, involving conformational changes of the head as well as surface regions that could potentially prevent RNA polymerase from docking to the ribosome.Under conditions of nutrient limitation, bacterial ribosomes undergo dimerization, forming a 100S complex that is translationally inactive. Here the authors present the structural basis for formation of the 100S complexes in Gram-positive bacteria, shedding light on the mechanism of translation suppression by the ribosome-silencing factors.

PubMed: 28959035
DOI: 10.1038/s41467-017-00753-8

実験手法

ELECTRON MICROSCOPY (2.9 Å)