1k3s: Difference between revisions

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[[Image:1k3s.png|left|200px]]
==Type III Secretion Chaperone SigE==
<StructureSection load='1k3s' size='340' side='right' caption='[[1k3s]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1k3s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K3S FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k3s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k3s RCSB], [http://www.ebi.ac.uk/pdbsum/1k3s PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_1k3s|  PDB=1k3s  |  SCENE=  }}
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<ref>PMID:11685226</ref>


===Type III Secretion Chaperone SigE===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_11685226}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1k3s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3S OCA].
</StructureSection>
 
[[Category: Bacillus cholerae-suis smith 1894]]
==Reference==
<ref group="xtra">PMID:011685226</ref><references group="xtra"/>
[[Category: Salmonella enterica]]
[[Category: Bertero, M G.]]
[[Category: Bertero, M G.]]
[[Category: Creagh, L.]]
[[Category: Creagh, L.]]

Revision as of 08:41, 8 June 2014

Type III Secretion Chaperone SigEType III Secretion Chaperone SigE

Structural highlights

1k3s is a 2 chain structure with sequence from "bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ 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. Structural and biochemical characterization of the type III secretion chaperones CesT and SigE. Nat Struct Biol. 2001 Dec;8(12):1031-6. PMID:11685226 doi:10.1038/nsb717

1k3s, resolution 1.90Å

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