6HTQ

Stringent response control by a bifunctional RelA enzyme in the presence and absence of the ribosome

これはPDB形式変換不可エントリーです。

6HTQ の概要

• エントリーDOI: 10.2210/pdb6htq/pdb
• EMDBエントリー: 0270
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L15, 50S ribosomal protein L16, ... (53 entities in total)
• 機能のキーワード: structure of bifunctional rel on b. subtilis 70s, ribosome
• 由来する生物種: Bacillus subtilis subsp. subtilis str. 168; 詳細
• タンパク質・核酸の鎖数: 53
• 化学式量合計: 2190608.52

構造登録者

Wilson, D.N.,Abdelshahid, M. (登録日: 2018-10-04, 公開日: 2019-10-23, 最終更新日: 2024-10-16)

主引用文献

Pausch, P.,Abdelshahid, M.,Steinchen, W.,Schafer, H.,Gratani, F.L.,Freibert, S.A.,Wolz, C.,Turgay, K.,Wilson, D.N.,Bange, G.
Structural Basis for Regulation of the Opposing (p)ppGpp Synthetase and Hydrolase within the Stringent Response Orchestrator Rel.
Cell Rep, 32:108157-108157, 2020

PubMed Abstract: The stringent response enables metabolic adaptation of bacteria under stress conditions and is governed by RelA/SpoT Homolog (RSH)-type enzymes. Long RSH-type enzymes encompass an N-terminal domain (NTD) harboring the second messenger nucleotide (p)ppGpp hydrolase and synthetase activity and a stress-perceiving and regulatory C-terminal domain (CTD). CTD-mediated binding of Rel to stalled ribosomes boosts (p)ppGpp synthesis. However, how the opposing activities of the NTD are controlled in the absence of stress was poorly understood. Here, we demonstrate on the RSH-type protein Rel that the critical regulative elements reside within the TGS (ThrRS, GTPase, and SpoT) subdomain of the CTD, which associates to and represses the synthetase to concomitantly allow for activation of the hydrolase. Furthermore, we show that Rel forms homodimers, which appear to control the interaction with deacylated-tRNA, but not the enzymatic activity of Rel. Collectively, our study provides a detailed molecular view into the mechanism of stringent response repression in the absence of stress.

PubMed: 32937119
DOI: 10.1016/j.celrep.2020.108157

実験手法

ELECTRON MICROSCOPY (4.5 Å)