1JYO

Structure of the Salmonella Virulence Effector SptP in Complex with its Secretion Chaperone SicP

1JYO の概要

• エントリーDOI: 10.2210/pdb1jyo/pdb
• 分子名称: SicP, protein tyrosine phosphatase SptP (3 entities in total)
• 機能のキーワード: salmonella, bacterial pathogenesis, infectious disease, virulence factor, type iii secretion, chaperone, unfolded, protein folding, sptp, sicp
• 由来する生物種: Salmonella typhimurium; 詳細
• 細胞内の位置: Cytoplasm: O85300; Secreted: P74873
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 81763.37

構造登録者

Stebbins, C.E.,Galan, J.E. (登録日: 2001-09-12, 公開日: 2001-11-07, 最終更新日: 2024-10-16)

主引用文献

Stebbins, C.E.,Galan, J.E.
Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion.
Nature, 414:77-81, 2001

PubMed Abstract: Many bacterial pathogens use a type III protein secretion system to deliver virulence effector proteins directly into the host cell cytosol, where they modulate cellular processes. A requirement for the effective translocation of several such effector proteins is the binding of specific cytosolic chaperones, which typically interact with discrete domains in the virulence factors. We report here the crystal structure at 1.9 A resolution of the chaperone-binding domain of the Salmonella effector protein SptP with its cognate chaperone SicP. The structure reveals that this domain is maintained in an extended, unfolded conformation that is wound around three successive chaperone molecules. Short segments from two different SptP molecules are juxtaposed by the chaperones, where they dimerize across a hydrophobic interface. These results imply that the chaperones associated with the type III secretion system maintain their substrates in a secretion-competent state that is capable of engaging the secretion machinery to travel through the type III apparatus in an unfolded or partially folded manner.

PubMed: 11689946
DOI: 10.1038/35102073

実験手法

X-RAY DIFFRACTION (1.9 Å)