1XOU

Crystal structure of the CesA-EspA complex

1XOU の概要

• エントリーDOI: 10.2210/pdb1xou/pdb
• 分子名称: EspA, Z5138 gene product (2 entities in total)
• 機能のキーワード: coiled coil, helix bundle, heterodimer, structural protein-chaperone complex, structural protein/chaperone
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31713.07

構造登録者

Yip, C.K.,Finlay, B.B.,Strynadka, N.C.J. (登録日: 2004-10-06, 公開日: 2004-12-28, 最終更新日: 2024-11-13)

主引用文献

Yip, C.K.,Finlay, B.B.,Strynadka, N.C.J.
Structural characterization of a type III secretion system filament protein in complex with its chaperone.
Nat.Struct.Mol.Biol., 12:75-81, 2005

PubMed Abstract: The type III secretion system (TTSS) mediates the specific translocation of bacterial proteins into the cytoplasm of eukaryotic cells, a process essential for the virulence of many Gram-negative pathogens. The enteropathogenic Escherichia coli TTSS protein EspA forms a hollow extracellular filament believed to be a molecular conduit for type III protein translocation. Structural analysis of EspA has been hampered by its polymeric nature. We show that EspA alone is sufficient to form filamentous structures in the absence of other pathogenicity island-encoded proteins. CesA is the recently proposed chaperone of EspA, and we demonstrate that CesA traps EspA in a monomeric state and inhibits its polymerization. Crystallographic analysis of the heterodimeric CesA-EspA complex at a resolution of 2.8 A reveals that EspA contains two long a-helices, which are involved in extensive coiled-coil interactions with CesA.

PubMed: 15619638
DOI: 10.1038/nsmb879

実験手法

X-RAY DIFFRACTION (2.8 Å)