2fm8: Difference between revisions

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[[Image:2fm8.gif|left|200px]]
{{Seed}}
[[Image:2fm8.png|left|200px]]


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{{STRUCTURE_2fm8|  PDB=2fm8  |  SCENE=  }}  
{{STRUCTURE_2fm8|  PDB=2fm8  |  SCENE=  }}  


'''Crystal Structure of the Salmonella Secretion Chaperone InvB in Complex with SipA'''
===Crystal Structure of the Salmonella Secretion Chaperone InvB in Complex with SipA===




==Overview==
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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.
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{{ABSTRACT_PUBMED_16507363}}


==About this Structure==
==About this Structure==
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[[Category: Type iii secretion]]
[[Category: Type iii secretion]]
[[Category: Virulence]]
[[Category: Virulence]]
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Revision as of 05:29, 29 July 2008

File:2fm8.png

Template:STRUCTURE 2fm8

Crystal Structure of the Salmonella Secretion Chaperone InvB in Complex with SipA

Template:ABSTRACT PUBMED 16507363

About this Structure

2FM8 is a Protein complex structure of sequences 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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