1k3s

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{{STRUCTURE_1k3s| PDB=1k3s | SCENE= }}
{{STRUCTURE_1k3s| PDB=1k3s | SCENE= }}
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'''Type III Secretion Chaperone SigE'''
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===Type III Secretion Chaperone SigE===
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==Overview==
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Several Gram-negative bacterial pathogens have evolved a type III secretion system to deliver virulence effector proteins directly into eukaryotic cells, a process essential for disease. This specialized secretion process requires customized chaperones specific for particular effector proteins. The crystal structures of the enterohemorrhagic Escherichia coli O157:H7 Tir-specific chaperone CesT and the Salmonella enterica SigD-specific chaperone SigE reveal a common overall fold and formation of homodimers. Site-directed mutagenesis suggests that variable, delocalized hydrophobic surfaces observed on the chaperone homodimers are responsible for specific binding to a particular effector protein. Isothermal titration calorimetry studies of Tir-CesT and enzymatic activity profiles of SigD-SigE indicate that the effector proteins are not globally unfolded in the presence of their cognate chaperones.
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==About this Structure==
==About this Structure==
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[[Category: Sige]]
[[Category: Sige]]
[[Category: Type iii]]
[[Category: Type iii]]
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Revision as of 00:48, 2 July 2008

Image:1k3s.png

Template:STRUCTURE 1k3s

Type III Secretion Chaperone SigE

Template:ABSTRACT PUBMED 11685226

About this Structure

1K3S is a Single protein structure of sequence from Salmonella enterica. Full crystallographic information is available from OCA.

Reference

Structural and biochemical characterization of the type III secretion chaperones CesT and SigE., Luo Y, Bertero MG, Frey EA, Pfuetzner RA, Wenk MR, Creagh L, Marcus SL, Lim D, Sicheri F, Kay C, Haynes C, Finlay BB, Strynadka NC, Nat Struct Biol. 2001 Dec;8(12):1031-6. PMID:11685226

Page seeded by OCA on Wed Jul 2 03:43:02 2008

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