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5klq

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<StructureSection load='5klq' size='340' side='right'caption='[[5klq]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='5klq' size='340' side='right'caption='[[5klq]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5klq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Psesy Psesy]. 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://proteopedia.org/fgij/fg.htm?mol=5KLQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5klq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._syringae Pseudomonas syringae pv. syringae]. 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 [https://proteopedia.org/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" id="ligandDat"><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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5klq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5klq OCA], [https://pdbe.org/5klq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5klq RCSB], [https://www.ebi.ac.uk/pdbsum/5klq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5klq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/HOZ1A_PSESY HOZ1A_PSESY] Serine/threonine-protein acetyltransferase translocated into infected cells, which impairs host microtubule network and host immunity by mediating acetylation of target proteins (PubMed:20636323, PubMed:22319451, PubMed:24204266, PubMed:27525589). Blocks secretion in host cells by mediating acetylation of host tubulin, thereby impairing host microbubule network (PubMed:22319451). Impairs host cell immunity by mediating acetylation of host TIFY/JAZ transcription repressors (Arabidopsis thaliana TIFY10B/JAZ2, TIFY11A/JAZ5, TIFY11B/JAZ6, TIFY5A/JAZ8, TIFY9/JAZ10 and TIFY3B/JAZ12), thereby activating host jasmonate signaling (PubMed:24204266, PubMed:27525589).<ref>PMID:20636323</ref> <ref>PMID:22319451</ref> <ref>PMID:24204266</ref> <ref>PMID:27525589</ref>
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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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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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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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<div class="pdbe-citations 5klq" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Psesy]]
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[[Category: Pseudomonas syringae pv. syringae]]
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[[Category: Song, J]]
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[[Category: Song J]]
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[[Category: Zhang, Z M]]
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[[Category: Zhang Z-M]]
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[[Category: Ser/thr acetyltransferase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of HopZ1a in complex with IP6 and CoA

PDB ID 5klq

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