5wez

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5wez" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5wez is ON HOLD until Paper Publication
+
==Structure of the Tir-CesT effector-chaperone complex==
-
 
+
<StructureSection load='5wez' size='340' side='right' caption='[[5wez]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
-
Authors:
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[5wez]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WEZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WEZ FirstGlance]. <br>
-
Description:
+
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wez OCA], [http://pdbe.org/5wez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wez RCSB], [http://www.ebi.ac.uk/pdbsum/5wez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wez ProSAT]</span></td></tr>
-
[[Category: Unreleased Structures]]
+
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/CEST_ECO27 CEST_ECO27]] Chaperone for the type III secretion of Tir. Probably stabilizes the protein, prevents inappropriate protein-proteininteractions and aids in secretion. [[http://www.uniprot.org/uniprot/TIR_ECO27 TIR_ECO27]] Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion. In strain E2348/69, acts mainly via the host adaptor proteins NCK1 and NCK2. Once clustered and phosphorylated at Tyr-474, Tir binds to NCK proteins, which in turn bind and activate host WASL/N-WASP, leading to actin polymerization. Can also trigger an inefficient, NCK-independent pedestal formation. This pathway involves phosphorylation of Tyr-454 and probably a putative host adaptor. Acts also via direct binding to the host cytoskeletal protein alpha-actinin in a NCK- and phosphotyrosine-independent manner. This interaction may stabilize the pedestal, but is not essential for its formation.<ref>PMID:10096089</ref> <ref>PMID:14757753</ref> <ref>PMID:14764108</ref> <ref>PMID:15813734</ref> <ref>PMID:17521329</ref> <ref>PMID:9390560</ref>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Coombes, B K]]
 +
[[Category: Little, D J]]
 +
[[Category: Chaperone]]
 +
[[Category: Complex]]
 +
[[Category: Effector]]
 +
[[Category: Secretion]]
 +
[[Category: Translocation]]

Revision as of 05:36, 11 July 2018

Structure of the Tir-CesT effector-chaperone complex

5wez, resolution 2.74Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5wez"
Personal tools