2zcv

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[[Image:2zcv.jpg|left|200px]]
 
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==Crystal structure of NADPH-dependent quinone oxidoreductase QOR2 complexed with NADPH from escherichia coli==
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The line below this paragraph, containing "STRUCTURE_2zcv", creates the "Structure Box" on the page.
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<StructureSection load='2zcv' size='340' side='right'caption='[[2zcv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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{{STRUCTURE_2zcv| PDB=2zcv | SCENE= }}
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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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'''Crystal structure of NADPH-dependent quinone oxidoreductase QOR2 complexed with NADPH from escherichia coli'''
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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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==Overview==
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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 ==
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.
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 [[Single protein]] structure of sequence from [http://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].
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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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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:[http://www.ncbi.nlm.nih.gov/pubmed/18455185 18455185]
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</div>
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<div class="pdbe-citations 2zcv" 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: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: NADPH:quinone reductase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cha SS]]
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[[Category: Cha, S S.]]
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[[Category: Kang SO]]
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[[Category: Kang, S O.]]
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[[Category: Kim DW]]
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[[Category: Kim, D W.]]
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[[Category: Kim IK]]
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[[Category: Kim, I K.]]
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[[Category: Kim MK]]
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[[Category: Kim, M K.]]
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[[Category: Kim YM]]
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[[Category: Kim, Y M.]]
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[[Category: Yim HS]]
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[[Category: Yim, H S.]]
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[[Category: Alpha-beta sandwich]]
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[[Category: Complex with nadph]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:18:13 2008''
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Current revision

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

PDB ID 2zcv

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