2fm9

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{{STRUCTURE_2fm9| PDB=2fm9 | SCENE= }}
{{STRUCTURE_2fm9| PDB=2fm9 | SCENE= }}
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'''Structure of Salmonella SipA residues 48-264'''
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===Structure of Salmonella SipA residues 48-264===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 16507363 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16507363}}
==About this Structure==
==About this Structure==
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[[Category: Type ii secretion]]
[[Category: Type ii secretion]]
[[Category: Virulence]]
[[Category: Virulence]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:03:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:23:12 2008''

Revision as of 10:23, 27 July 2008

Template:STRUCTURE 2fm9

Structure of Salmonella SipA residues 48-264

Template:ABSTRACT PUBMED 16507363

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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