9GFT

Structure of the HrpA-bound E. coli disome, Class I

これはPDB形式変換不可エントリーです。

9GFT の概要

• エントリーDOI: 10.2210/pdb9gft/pdb
• EMDBエントリー: 51318
• 分子名称: 16S ribosomal RNA, Small ribosomal subunit protein uS10, A-site tRNA, ... (63 entities in total)
• 機能のキーワード: ribosome, rna helicase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 116
• 化学式量合計: 4870071.38

構造登録者

Esser, H.F.,Berninghausen, O.,Becker, T.,Beckmann, R. (登録日: 2024-08-12, 公開日: 2025-02-12, 最終更新日: 2025-03-19)

主引用文献

Campbell, A.,Esser, H.F.,Burroughs, A.M.,Berninghausen, O.,Aravind, L.,Becker, T.,Green, R.,Beckmann, R.,Buskirk, A.R.
The RNA helicase HrpA rescues collided ribosomes in E. coli.
Mol.Cell, 85:999-1007.e7, 2025

PubMed Abstract: Although many antibiotics inhibit bacterial ribosomes, the loss of known factors that rescue stalled ribosomes does not lead to robust antibiotic sensitivity in E. coli, suggesting the existence of additional mechanisms. Here, we show that the RNA helicase HrpA rescues stalled ribosomes in E. coli. Acting selectively on ribosomes that have collided, HrpA uses ATP hydrolysis to split stalled ribosomes into subunits. Cryoelectron microscopy (cryo-EM) structures reveal how HrpA simultaneously binds to two collided ribosomes, explaining its selectivity, and how its helicase module engages downstream mRNA such that, by exerting a pulling force on the mRNA, it would destabilize the stalled ribosome. These studies show that ribosome splitting is a conserved mechanism that allows proteobacteria to tolerate ribosome-targeting antibiotics.

PubMed: 39922193
DOI: 10.1016/j.molcel.2025.01.018

実験手法

ELECTRON MICROSCOPY (3.1 Å)