4ci6: Difference between revisions
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<StructureSection load='4ci6' size='340' side='right'caption='[[4ci6]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='4ci6' size='340' side='right'caption='[[4ci6]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ci6]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ci6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda] and [https://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CI6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.651Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ci6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ci6 OCA], [https://pdbe.org/4ci6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ci6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ci6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ci6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G3CKA6_SPOFR G3CKA6_SPOFR] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Spodoptera frugiperda]] | [[Category: Spodoptera frugiperda]] | ||
[[Category: | [[Category: Yersinia enterocolitica]] | ||
[[Category: | [[Category: Grimes JM]] | ||
[[Category: | [[Category: Lee WL]] | ||
[[Category: | [[Category: Robinson RC]] | ||
Latest revision as of 15:10, 20 December 2023
Mechanisms of crippling actin-dependent phagocytosis by YopOMechanisms of crippling actin-dependent phagocytosis by YopO
Structural highlights
FunctionPublication Abstract from PubMedPathogenic Yersinia species evade host immune systems through the injection of Yersinia outer proteins (Yops) into phagocytic cells. One Yop, YopO, also known as YpkA, induces actin-filament disruption, impairing phagocytosis. Here we describe the X-ray structure of Yersinia enterocolitica YopO in complex with actin, which reveals that YopO binds to an actin monomer in a manner that blocks polymerization yet allows the bound actin to interact with host actin-regulating proteins. SILAC-MS and biochemical analyses confirm that actin-polymerization regulators such as VASP, EVL, WASP, gelsolin and the formin diaphanous 1 are directly sequestered and phosphorylated by YopO through formation of ternary complexes with actin. This leads to a model in which YopO at the membrane sequesters actin from polymerization while using the bound actin as bait to recruit, phosphorylate and misregulate host actin-regulating proteins to disrupt phagocytosis. Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization.,Lee WL, Grimes JM, Robinson RC Nat Struct Mol Biol. 2015 Feb 9. doi: 10.1038/nsmb.2964. PMID:25664724[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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