2FM8

Crystal Structure of the Salmonella Secretion Chaperone InvB in Complex with SipA

2FM8 の概要

• エントリーDOI: 10.2210/pdb2fm8/pdb
• 分子名称: Surface presentation of antigens protein spaK, Cell invasion protein sipA (3 entities in total)
• 機能のキーワード: type iii secretion, chaperone, translocation, protein folding, virulence, salmonella, bacterial, chaperone-cell invasion complex, chaperone/cell invasion
• 由来する生物種: Salmonella typhimurium; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 55931.15

構造登録者

Lilic, M.,Vujanac, M.,Stebbins, C.E. (登録日: 2006-01-08, 公開日: 2006-03-21, 最終更新日: 2024-02-14)

主引用文献

Lilic, M.,Vujanac, M.,Stebbins, C.E.
A common structural motif in the binding of virulence factors to bacterial secretion chaperones.
Mol.Cell, 21:653-664, 2006

PubMed Abstract: Salmonella invasion protein A (SipA) is translocated into host cells by a type III secretion system (T3SS) and comprises two regions: one domain binds its cognate type III secretion chaperone, InvB, in the bacterium to facilitate translocation, while a second domain functions in the host cell, contributing to bacterial uptake by polymerizing actin. We present here the crystal structures of the SipA chaperone binding domain (CBD) alone and in complex with InvB. The SipA CBD is found to consist of a nonglobular polypeptide as well as a large globular domain, both of which are necessary for binding to InvB. We also identify a structural motif that may direct virulence factors to their cognate chaperones in a diverse range of pathogenic bacteria. Disruption of this structural motif leads to a destabilization of several chaperone-substrate complexes from different species, as well as an impairment of secretion in Salmonella.

PubMed: 16507363
DOI: 10.1016/j.molcel.2006.01.026

実験手法

X-RAY DIFFRACTION (2.2 Å)