2fm9
From Proteopedia
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| - | [[Image:2fm9.gif|left|200px]] | + | [[Image:2fm9.gif|left|200px]] |
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| - | '''Structure of Salmonella SipA residues 48-264''' | + | {{Structure |
| + | |PDB= 2fm9 |SIZE=350|CAPTION= <scene name='initialview01'>2fm9</scene>, resolution 2.000Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= sipA, sspA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of Salmonella SipA residues 48-264''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FM9 is a [ | + | 2FM9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FM9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16507363 16507363] |
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: virulence]] | [[Category: virulence]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:54:07 2008'' |
Revision as of 14:54, 20 March 2008
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| , resolution 2.000Å | |||||||
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| Gene: | sipA, sspA (Salmonella typhimurium) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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