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{{STRUCTURE_2zcv|  PDB=2zcv  |  SCENE=  }}
==Crystal structure of NADPH-dependent quinone oxidoreductase QOR2 complexed with NADPH from escherichia coli==
===Crystal structure of NADPH-dependent quinone oxidoreductase QOR2 complexed with NADPH from escherichia coli===
<StructureSection load='2zcv' size='340' side='right' caption='[[2zcv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
{{ABSTRACT_PUBMED_18455185}}
== Structural highlights ==
<table><tr><td colspan='2'>[[2zcv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZCV FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zcu|2zcu]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH:quinone_reductase NADPH:quinone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.5 1.6.5.5] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zcv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zcv RCSB], [http://www.ebi.ac.uk/pdbsum/2zcv PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zc/2zcv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Function==
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>
[[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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[2zcv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCV OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018455185</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: NADPH:quinone reductase]]
[[Category: NADPH:quinone reductase]]
[[Category: Cha, S S.]]
[[Category: Cha, S S.]]

Revision as of 05:21, 3 October 2014

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

2zcv, resolution 2.30Å

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