2zcv

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{{STRUCTURE_2zcv| PDB=2zcv | SCENE= }}
 
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===Crystal structure of NADPH-dependent quinone oxidoreductase QOR2 complexed with NADPH from escherichia coli===
 
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{{ABSTRACT_PUBMED_18455185}}
 
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==Function==
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==Crystal structure of NADPH-dependent quinone oxidoreductase QOR2 complexed with NADPH from escherichia coli==
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[[http://www.uniprot.org/uniprot/QOR2_ECOLI QOR2_ECOLI]] Quinone oxidoreductase that may play some additional role beyond quinone reduction. Potential redox sensor protein. Overexpression induces retardation of growth.
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<StructureSection load='2zcv' size='340' side='right'caption='[[2zcv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2zcv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZCV 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]] 2.3&#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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2zcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zcv OCA], [https://pdbe.org/2zcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zcv RCSB], [https://www.ebi.ac.uk/pdbsum/2zcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zcv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/QOR2_ECOLI QOR2_ECOLI] Quinone oxidoreductase that may play some additional role beyond quinone reduction. Potential redox sensor protein. Overexpression induces retardation of growth.
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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/zc/2zcv_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=2zcv 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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Escherichia coli QOR2 [NAD(P)H-dependent quinone oxidoreductase; a ytfG gene product], which catalyzes two-electron reduction of methyl-1,4-benzoquinone, is a new type of quinone-reducing enzyme with distinct primary sequence and oligomeric conformation from previously known quinone oxidoreductases. The crystal structures of native QOR2 and the QOR2-NADPH (nicotinamide adenine dinucleotide phosphate, reduced form) complex reveal that QOR2 consists of two domains (N-domain and C-domain) resembling those of NmrA, a negative transcriptional regulator that belongs to the short-chain dehydrogenase/reductase family. The N-domain, which adopts the Rossmann fold, provides a platform for NADPH binding, whereas the C-domain, which contains a hydrophobic pocket connected to the NADPH-binding site, appears to play important roles in substrate binding. Asn143 near the NADPH-binding site has been identified to be involved in substrate binding and catalysis from structural and mutational analyses. Moreover, compared with wild-type strain, the qor2-overexpressing strain shows growth retardation and remarkable decrease in several enzymes involved in carbon metabolism, suggesting that QOR2 could play some physiological roles in addition to quinone reduction.
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==About this Structure==
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Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from Escherichia coli.,Kim IK, Yim HS, Kim MK, Kim DW, Kim YM, Cha SS, Kang SO J Mol Biol. 2008 May 30;379(2):372-84. Epub 2008 Apr 8. PMID:18455185<ref>PMID:18455185</ref>
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[[2zcv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCV OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:018455185</ref><references group="xtra"/><references/>
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</div>
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[[Category: NADPH:quinone reductase]]
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<div class="pdbe-citations 2zcv" style="background-color:#fffaf0;"></div>
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[[Category: Cha, S S.]]
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== References ==
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[[Category: Kang, S O.]]
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<references/>
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[[Category: Kim, D W.]]
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__TOC__
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[[Category: Kim, I K.]]
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</StructureSection>
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[[Category: Kim, M K.]]
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[[Category: Escherichia coli]]
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[[Category: Kim, Y M.]]
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[[Category: Large Structures]]
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[[Category: Yim, H S.]]
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[[Category: Cha SS]]
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[[Category: Alpha-beta sandwich]]
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[[Category: Kang SO]]
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[[Category: Complex with nadph]]
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[[Category: Kim DW]]
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[[Category: Oxidoreductase]]
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[[Category: Kim IK]]
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[[Category: Kim MK]]
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[[Category: Kim YM]]
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[[Category: Yim HS]]

Current revision

Crystal structure of NADPH-dependent quinone oxidoreductase QOR2 complexed with NADPH from escherichia coli

PDB ID 2zcv

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