1P5V

X-ray structure of the Caf1M:Caf1 chaperone:subunit preassembly complex

1P5V の概要

• エントリーDOI: 10.2210/pdb1p5v/pdb
• 関連するPDBエントリー: 1P5U
• 分子名称: Chaperone protein Caf1M, F1 capsule antigen (3 entities in total)
• 機能のキーワード: chaperone, chaperone-target complex, chaperone-subunit complex, protein fiber, donor strand complementation, donor strand exchange, structural protein
• 由来する生物種: Yersinia pestis; 詳細
• 細胞内の位置: Periplasm: P26926; Secreted, capsule: P26948
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42002.24

構造登録者

Zavialov, A.V.,Berglund, J.,Pudney, A.F.,Fooks, L.J.,Ibrahim, T.M.,MacIntyre, S.,Knight, S.D. (登録日: 2003-04-28, 公開日: 2003-06-24, 最終更新日: 2024-11-06)

主引用文献

Zavialov, A.V.,Berglund, J.,Pudney, A.F.,Fooks, L.J.,Ibrahim, T.M.,MacIntyre, S.,Knight, S.D.
Structure and Biogenesis of the Capsular F1 Antigen from Yersinia pestis. Preserved Folding Energy Drives Fiber Formation
Cell(Cambridge,Mass.), 113:587-596, 2003

PubMed Abstract: Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation.

PubMed: 12787500
DOI: 10.1016/S0092-8674(03)00351-9

実験手法

X-RAY DIFFRACTION (1.7 Å)