1k3e
From Proteopedia
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| - | [[Image:1k3e.jpg|left|200px]] | + | [[Image:1k3e.jpg|left|200px]] |
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| - | '''Type III secretion chaperone CesT''' | + | {{Structure |
| + | |PDB= 1k3e |SIZE=350|CAPTION= <scene name='initialview01'>1k3e</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Type III secretion chaperone CesT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K3E is a [ | + | 1K3E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3E OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11685226 11685226] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: type iii]] | [[Category: type iii]] | ||
| - | ''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 12:12:03 2008'' |
Revision as of 10:12, 20 March 2008
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Type III secretion chaperone CesT
Overview
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.
About this Structure
1K3E is a Single protein structure of sequence from Escherichia coli. 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
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