1jyo
From Proteopedia
(New page: 200px<br /><applet load="1jyo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jyo, resolution 1.9Å" /> '''Structure of the Salm...) |
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| - | [[Image:1jyo.gif|left|200px]]<br /><applet load="1jyo" size=" | + | [[Image:1jyo.gif|left|200px]]<br /><applet load="1jyo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jyo, resolution 1.9Å" /> | caption="1jyo, resolution 1.9Å" /> | ||
'''Structure of the Salmonella Virulence Effector SptP in Complex with its Secretion Chaperone SicP'''<br /> | '''Structure of the Salmonella Virulence Effector SptP in Complex with its Secretion Chaperone SicP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many bacterial pathogens use a type III protein secretion system to | + | 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== | ==About this Structure== | ||
| - | 1JYO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http:// | + | 1JYO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1JYO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
| - | [[Category: Galan, J | + | [[Category: Galan, J E.]] |
| - | [[Category: Stebbins, C | + | [[Category: Stebbins, C E.]] |
[[Category: bacterial pathogenesis]] | [[Category: bacterial pathogenesis]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
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[[Category: virulence factor]] | [[Category: virulence factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:11 2008'' |
Revision as of 11:28, 21 February 2008
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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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