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5wez

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m (Protected "5wez" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5wez is ON HOLD until Paper Publication
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==Structure of the Tir-CesT effector-chaperone complex==
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<StructureSection load='5wez' size='340' side='right' caption='[[5wez]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<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>
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Description:
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</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>
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[[Category: Unreleased Structures]]
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</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Coombes, B K]]
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[[Category: Little, D J]]
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[[Category: Chaperone]]
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[[Category: Complex]]
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[[Category: Effector]]
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[[Category: Secretion]]
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[[Category: Translocation]]

Revision as of 05:36, 11 July 2018

Structure of the Tir-CesT effector-chaperone complex

5wez, resolution 2.74Å

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