2fm9
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(New page: 200px<br /><applet load="2fm9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fm9, resolution 2.000Å" /> '''Structure of Salmon...)
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Revision as of 08:30, 21 November 2007
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Structure of Salmonella SipA residues 48-264
Overview
Salmonella invasion protein A (SipA) is translocated into host cells by a, type III secretion system (T3SS) and comprises two regions: one domain, binds its cognate type III secretion chaperone, InvB, in the bacterium to, facilitate translocation, while a second domain functions in the host, cell, contributing to bacterial uptake by polymerizing actin. We present, here the crystal structures of the SipA chaperone binding domain (CBD), alone and in complex with InvB. The SipA CBD is found to consist of a, nonglobular polypeptide as well as a large globular domain, both of which, are necessary for binding to InvB. We also identify a structural motif, that may direct virulence factors to their cognate chaperones in a diverse, range of pathogenic bacteria. Disruption of this structural motif leads to, a destabilization of several chaperone-substrate complexes from different, species, as well as an impairment of secretion in Salmonella.
About this Structure
2FM9 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
A common structural motif in the binding of virulence factors to bacterial secretion chaperones., Lilic M, Vujanac M, Stebbins CE, Mol Cell. 2006 Mar 3;21(5):653-64. PMID:16507363
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