1xou
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(New page: 200px<br /><applet load="1xou" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xou, resolution 2.80Å" /> '''Crystal structure of...)
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Revision as of 00:29, 25 November 2007
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Crystal structure of the CesA-EspA complex
Overview
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.
About this Structure
1XOU is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural characterization of a type III secretion system filament protein in complex with its chaperone., Yip CK, Finlay BB, Strynadka NC, Nat Struct Mol Biol. 2005 Jan;12(1):75-81. Epub 2004 Dec 26. PMID:15619638
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