1jyo
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyo OCA], [http://www.ebi.ac.uk/pdbsum/1jyo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jyo RCSB]</span> | ||
}} | }} | ||
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[[Category: virulence factor]] | [[Category: virulence factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:40:51 2008'' |
Revision as of 18:40, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the Salmonella Virulence Effector SptP in Complex with its Secretion Chaperone SicP
Overview
Many bacterial pathogens use a type III protein secretion system to deliver virulence effector proteins directly into the host cell cytosol, where they modulate cellular processes. A requirement for the effective translocation of several such effector proteins is the binding of specific cytosolic chaperones, which typically interact with discrete domains in the virulence factors. We report here the crystal structure at 1.9 A resolution of the chaperone-binding domain of the Salmonella effector protein SptP with its cognate chaperone SicP. The structure reveals that this domain is maintained in an extended, unfolded conformation that is wound around three successive chaperone molecules. Short segments from two different SptP molecules are juxtaposed by the chaperones, where they dimerize across a hydrophobic interface. These results imply that the chaperones associated with the type III secretion system maintain their substrates in a secretion-competent state that is capable of engaging the secretion machinery to travel through the type III apparatus in an unfolded or partially folded manner.
About this Structure
1JYO is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion., Stebbins CE, Galan JE, Nature. 2001 Nov 1;414(6859):77-81. PMID:11689946
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