1XOU

Crystal structure of the CesA-EspA complex

Summary for 1XOU

• Entry DOI: 10.2210/pdb1xou/pdb
• Descriptor: EspA, Z5138 gene product (2 entities in total)
• Functional Keywords: coiled coil, helix bundle, heterodimer, structural protein-chaperone complex, structural protein/chaperone
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 31713.07

Authors

Yip, C.K.,Finlay, B.B.,Strynadka, N.C.J. (deposition date: 2004-10-06, release date: 2004-12-28, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)