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{{Seed}}
[[Image:1k3s.png|left|200px]]


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==Type III Secretion Chaperone SigE==
The line below this paragraph, containing "STRUCTURE_1k3s", creates the "Structure Box" on the page.
<StructureSection load='1k3s' size='340' side='right'caption='[[1k3s]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1k3s]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K3S FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k3s OCA], [https://pdbe.org/1k3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k3s RCSB], [https://www.ebi.ac.uk/pdbsum/1k3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k3s ProSAT]</span></td></tr>
{{STRUCTURE_1k3s|  PDB=1k3s  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0F6AZQ4_SALT1 A0A0F6AZQ4_SALT1]
<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.


===Type III Secretion Chaperone SigE===
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>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
The line below this paragraph, {{ABSTRACT_PUBMED_11685226}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1k3s" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 11685226 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_11685226}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1K3S is a [[Single protein]] structure of 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].
 
==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://www.ncbi.nlm.nih.gov/pubmed/11685226 11685226]
[[Category: Salmonella enterica]]
[[Category: Salmonella enterica]]
[[Category: Single protein]]
[[Category: Bertero MG]]
[[Category: Bertero, M G.]]
[[Category: Creagh L]]
[[Category: Creagh, L.]]
[[Category: Finlay BB]]
[[Category: Finlay, B B.]]
[[Category: Frey EA]]
[[Category: Frey, E A.]]
[[Category: Lim D]]
[[Category: Lim, D.]]
[[Category: Luo Y]]
[[Category: Luo, Y.]]
[[Category: Marcus SL]]
[[Category: Marcus, S L.]]
[[Category: Pfuetzner RA]]
[[Category: Pfuetzner, R A.]]
[[Category: Strynadka NCJ]]
[[Category: Strynadka, N C.J.]]
[[Category: Wenk MR]]
[[Category: Wenk, M R.]]
[[Category: Chaperone]]
[[Category: Secretion]]
[[Category: Sige]]
[[Category: Type iii]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 03:43:02 2008''

Latest revision as of 13:00, 21 June 2023

Type III Secretion Chaperone SigEType III Secretion Chaperone SigE

Structural highlights

1k3s is a 2 chain structure with sequence from Salmonella enterica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0F6AZQ4_SALT1

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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