5MTW

Mycobacterium tuberculosis Rv1957 SecB-like chaperone in complex with a ChAD peptide from Rv1956 HigA1 antitoxin

5MTW の概要

• エントリーDOI: 10.2210/pdb5mtw/pdb
• 分子名称: SecB-like chaperone Rv1957, Antitoxin HigA1, DIMETHYL SULFOXIDE, ... (5 entities in total)
• 機能のキーワード: toxin-antitoxin-chaperone system, complex, chaperone
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 86687.22

構造登録者

Guillet, V.,Mourey, L. (登録日: 2017-01-10, 公開日: 2018-10-24, 最終更新日: 2024-01-17)

主引用文献

Guillet, V.,Bordes, P.,Bon, C.,Marcoux, J.,Gervais, V.,Sala, A.J.,Dos Reis, S.,Slama, N.,Mares-Mejia, I.,Cirinesi, A.M.,Maveyraud, L.,Genevaux, P.,Mourey, L.
Structural insights into chaperone addiction of toxin-antitoxin systems.
Nat Commun, 10:782-782, 2019

PubMed Abstract: SecB chaperones assist protein export by binding both unfolded proteins and the SecA motor. Certain SecB homologs can also control toxin-antitoxin (TA) systems known to modulate bacterial growth in response to stress. In such TA-chaperone (TAC) systems, SecB assists the folding and prevents degradation of the antitoxin, thus facilitating toxin inhibition. Chaperone dependency is conferred by a C-terminal extension in the antitoxin known as chaperone addiction (ChAD) sequence, which makes the antitoxin aggregation-prone and prevents toxin inhibition. Using TAC of Mycobacterium tuberculosis, we present the structure of a SecB-like chaperone bound to its ChAD peptide. We find differences in the binding interfaces when compared to SecB-SecA or SecB-preprotein complexes, and show that the antitoxin can reach a functional form while bound to the chaperone. This work reveals how chaperones can use discrete surface binding regions to accommodate different clients or partners and thereby expand their substrate repertoire and functions.

PubMed: 30770830
DOI: 10.1038/s41467-019-08747-4

実験手法

X-RAY DIFFRACTION (1.84 Å)