3jyn

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{{STRUCTURE_3jyn| PDB=3jyn | SCENE= }}
 
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===Crystal structures of Pseudomonas syringae pv. Tomato DC3000 quinone oxidoreductase complexed with NADPH===
 
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{{ABSTRACT_PUBMED_19818736}}
 
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==About this Structure==
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==Crystal structures of Pseudomonas syringae pv. Tomato DC3000 quinone oxidoreductase complexed with NADPH==
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[[3jyn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JYN OCA].
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<StructureSection load='3jyn' size='340' side='right'caption='[[3jyn]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3jyn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JYN FirstGlance]. <br>
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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]] 2.01&#8491;</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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></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=3jyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jyn OCA], [https://pdbe.org/3jyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jyn RCSB], [https://www.ebi.ac.uk/pdbsum/3jyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jyn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q88B47_PSESM Q88B47_PSESM]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jy/3jyn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3jyn ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Zeta-crystallin-like quinone oxidoreductase is NAD(P)H-dependent and catalyzes one-electron reduction of certain quinones to generate semiquinone. Here we present the crystal structures of zeta-crystallin-like quinone oxidoreductase from Pseudomonas syringae pv. tomato DC3000 (PtoQOR) and its complexes with NADPH determined at 2.4 and 2.01A resolutions, respectively. PtoQOR forms as a homologous dimer, each monomer containing two domains. In the structure of the PtoQOR-NADPH complex, NADPH locates in the groove between the two domains. NADPH binding causes obvious conformational changes in the structure of PtoQOR. The putative substrate-binding site of PtoQOR is wider than that of Escherichia coli and Thermus thermophilus HB8. Activity assays show that PtoQOR has weak 1,4-benzoquinone catalytic activity, and very strong reduction activity towards large substrates such as 9,10-phenanthrenequinone. We propose a model to explain the conformational changes which take place during reduction reactions catalyzed by PtoQOR.
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==Reference==
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Crystal structures of Pseudomonas syringae pv. tomato DC3000 quinone oxidoreductase and its complex with NADPH.,Pan X, Zhang H, Gao Y, Li M, Chang W Biochem Biophys Res Commun. 2009 Dec 18;390(3):597-602. Epub 2009 Oct 8. PMID:19818736<ref>PMID:19818736</ref>
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<ref group="xtra">PMID:019818736</ref><references group="xtra"/><references/>
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[[Category: NADPH:quinone reductase]]
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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 3jyn" 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>
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[[Category: Large Structures]]
[[Category: Pseudomonas syringae pv. tomato]]
[[Category: Pseudomonas syringae pv. tomato]]
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[[Category: Chang, W.]]
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[[Category: Chang W]]
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[[Category: Gao, Y.]]
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[[Category: Gao Y]]
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[[Category: Li, M.]]
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[[Category: Li M]]
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[[Category: Pan, X.]]
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[[Category: Pan X]]
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[[Category: Zhang, H.]]
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[[Category: Zhang H]]
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[[Category: Oxidoreductase]]
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[[Category: Protein-nadph complex]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structures of Pseudomonas syringae pv. Tomato DC3000 quinone oxidoreductase complexed with NADPH

PDB ID 3jyn

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