4PU3

Shewanella oneidensis MR-1 Toxin Antitoxin System HipA, HipB and its operator DNA complex (space group P212121)

4PU3 の概要

• エントリーDOI: 10.2210/pdb4pu3/pdb
• 関連するPDBエントリー: 4PU4 4PU5
• 分子名称: Toxin-antitoxin system toxin HipA family, Toxin-antitoxin system antidote transcriptional repressor Xre family, Operator DNA, ... (4 entities in total)
• 機能のキーワード: toxin antitoxin system, toxin-antitoxin-dna complex, toxin/antitoxin/dna
• 由来する生物種: Shewanella oneidensis; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 144207.75

構造登録者

Wen, Y.,Behiels, E.,Felix, J.,Elegheert, J.,Vergauwen, B.,Devreese, B.,Savvides, S. (登録日: 2014-03-12, 公開日: 2014-08-06, 最終更新日: 2024-11-06)

主引用文献

Wen, Y.,Behiels, E.,Felix, J.,Elegheert, J.,Vergauwen, B.,Devreese, B.,Savvides, S.N.
The bacterial antitoxin HipB establishes a ternary complex with operator DNA and phosphorylated toxin HipA to regulate bacterial persistence.
Nucleic Acids Res., 42:10134-10147, 2014

PubMed Abstract: Nearly all bacteria exhibit a type of phenotypic growth described as persistence that is thought to underlie antibiotic tolerance and recalcitrant chronic infections. The chromosomally encoded high-persistence (Hip) toxin-antitoxin proteins HipASO and HipBSO from Shewanella oneidensis, a proteobacterium with unusual respiratory capacities, constitute a type II toxin-antitoxin protein module. Here we show that phosphorylated HipASO can engage in an unexpected ternary complex with HipBSO and double-stranded operator DNA that is distinct from the prototypical counterpart complex from Escherichia coli. The structure of HipBSO in complex with operator DNA reveals a flexible C-terminus that is sequestered by HipASO in the ternary complex, indicative of its role in binding HipASO to abolish its function in persistence. The structure of HipASO in complex with a non-hydrolyzable ATP analogue shows that HipASO autophosphorylation is coupled to an unusual conformational change of its phosphorylation loop. However, HipASO is unable to phosphorylate the translation factor Elongation factor Tu, contrary to previous reports, but in agreement with more recent findings. Our studies suggest that the phosphorylation state of HipA is an important factor in persistence and that the structural and mechanistic diversity of HipAB modules as regulatory factors in bacterial persistence is broader than previously thought.

PubMed: 25056321
DOI: 10.1093/nar/gku665

実験手法

X-RAY DIFFRACTION (3.39 Å)