5cpc: Difference between revisions
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''' | ==Crystal structure of SopD, a type III secreted virulence effector from Salmonella enterica== | ||
<StructureSection load='5cpc' size='340' side='right' caption='[[5cpc]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cq9|5cq9]]</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=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> | |||
</table> | |||
== Function == | |||
[[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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Structural genomic]] | |||
[[Category: Cygler, M]] | [[Category: Cygler, M]] | ||
[[Category: Shi, R]] | [[Category: Shi, R]] | ||
[[Category: Bsgi]] | |||
[[Category: Cell invasion]] | |||
[[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
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