5cpc

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'''Unreleased structure'''
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==Crystal structure of SopD, a type III secreted virulence effector from Salmonella enterica==
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<StructureSection load='5cpc' size='340' side='right' caption='[[5cpc]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5cpc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CPC FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cq9|5cq9]]</td></tr>
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<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=5cpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cpc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5cpc RCSB], [http://www.ebi.ac.uk/pdbsum/5cpc PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SOPD_SALTY SOPD_SALTY]] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Contributes to replication in macrophages. Plays a role, cooperatively with SopB, in membrane fission and macropinosome formation during invasion.<ref>PMID:15554961</ref> <ref>PMID:17696999</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Intracellular bacterial pathogens of a diverse nature share the ability to evade host immunity by impairing trafficking of endocytic cargo to lysosomes for degradation, a process that is poorly understood. Here, we show that the Salmonella enterica type 3 secreted effector SopD2 mediates this process by binding the host regulatory GTPase Rab7 and inhibiting its nucleotide exchange. Consequently, this limits Rab7 interaction with its dynein- and kinesin-binding effectors RILP and FYCO1 and thereby disrupts host-driven regulation of microtubule motors. Our study identifies a bacterial effector capable of directly binding and thereby modulating Rab7 activity and a mechanism of endocytic trafficking disruption that may provide insight into the pathogenesis of other bacteria. Additionally, we provide a powerful tool for the study of Rab7 function, and a potential therapeutic target.
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The entry 5cpc is ON HOLD until Paper Publication
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Salmonella Disrupts Host Endocytic Trafficking by SopD2-Mediated Inhibition of Rab7.,D'Costa VM, Braun V, Landekic M, Shi R, Proteau A, McDonald L, Cygler M, Grinstein S, Brumell JH Cell Rep. 2015 Sep 1;12(9):1508-18. doi: 10.1016/j.celrep.2015.07.063. Epub 2015 , Aug 20. PMID:26299973<ref>PMID:26299973</ref>
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Authors: Shi, R., Cygler, M., Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of SopD, a type III secreted virulence effector from Salmonella enterica
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Montreal-Kingston Bacterial Structural Genomics Initiative (Bsgi)]]
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__TOC__
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</StructureSection>
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[[Category: Structural genomic]]
[[Category: Cygler, M]]
[[Category: Cygler, M]]
[[Category: Shi, R]]
[[Category: Shi, R]]
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[[Category: Bsgi]]
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[[Category: Cell invasion]]
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[[Category: T3ss effector protein]]

Revision as of 11:12, 9 September 2015

Crystal structure of SopD, a type III secreted virulence effector from Salmonella enterica

5cpc, resolution 2.15Å

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