5klq

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m (Protected "5klq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5klq is ON HOLD until Paper Publication
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==Crystal structure of HopZ1a in complex with IP6 and CoA==
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<StructureSection load='5klq' size='340' side='right' caption='[[5klq]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5klq]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KLQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KLQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5klp|5klp]]</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=5klq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5klq OCA], [http://pdbe.org/5klq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5klq RCSB], [http://www.ebi.ac.uk/pdbsum/5klq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5klq ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Effectors secreted by the type III secretion system are essential for bacterial pathogenesis. Members of the Yersinia outer-protein J (YopJ) family of effectors found in diverse plant and animal pathogens depend on a protease-like catalytic triad to acetylate host proteins and produce virulence. However, the structural basis for this noncanonical acetyltransferase activity remains unknown. Here, we report the crystal structures of the YopJ effector HopZ1a, produced by the phytopathogen Pseudomonas syringae, in complex with the eukaryote-specific cofactor inositol hexakisphosphate (IP6) and/or coenzyme A (CoA). Structural, computational and functional characterizations reveal a catalytic core with a fold resembling that of ubiquitin-like cysteine proteases and an acetyl-CoA-binding pocket formed after IP6-induced structural rearrangements. Modeling-guided mutagenesis further identified key IP6-interacting residues of Salmonella effector AvrA that are required for acetylating its substrate. Our study reveals the structural basis of a novel class of acetyltransferases and the conserved allosteric regulation of YopJ effectors by IP6.
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Authors: Zhang, Z.-M., Song, J.
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Structure of a pathogen effector reveals the enzymatic mechanism of a novel acetyltransferase family.,Zhang ZM, Ma KW, Yuan S, Luo Y, Jiang S, Hawara E, Pan S, Ma W, Song J Nat Struct Mol Biol. 2016 Aug 15. doi: 10.1038/nsmb.3279. PMID:27525589<ref>PMID:27525589</ref>
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Description: Crystal structure of HopZ1a in complex with IP6 and CoA
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Zhang, Z.-M]]
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<div class="pdbe-citations 5klq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Song, J]]
[[Category: Song, J]]
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[[Category: Zhang, Z M]]
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[[Category: Ser/thr acetyltransferase]]
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[[Category: Transferase]]

Revision as of 05:11, 9 September 2016

Crystal structure of HopZ1a in complex with IP6 and CoA

5klq, resolution 3.40Å

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