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| | ==Crystal structure of Saccharomyces cerevisiae Zeta-crystallin-like quinone oxidoreductase Zta1== | | ==Crystal structure of Saccharomyces cerevisiae Zeta-crystallin-like quinone oxidoreductase Zta1== |
| - | <StructureSection load='3qwa' size='340' side='right' caption='[[3qwa]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3qwa' size='340' side='right'caption='[[3qwa]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qwa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QWA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qwa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QWA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qwb|3qwb]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YBR0421, YBR046C, ZTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qwa OCA], [https://pdbe.org/3qwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qwa RCSB], [https://www.ebi.ac.uk/pdbsum/3qwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qwa ProSAT]</span></td></tr> |
| - | <tr id='activity'><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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qwa OCA], [http://pdbe.org/3qwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qwa RCSB], [http://www.ebi.ac.uk/pdbsum/3qwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qwa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/QOR_YEAST QOR_YEAST] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: NADPH:quinone reductase]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Bao, Z Z]] | + | [[Category: Bao ZZ]] |
| - | [[Category: Chen, Y X]] | + | [[Category: Chen YX]] |
| - | [[Category: Guo, P C]] | + | [[Category: Guo PC]] |
| - | [[Category: Ma, X X]] | + | [[Category: Ma XX]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Cytoplasm and nucleus]]
| + | |
| - | [[Category: Nadph binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Quinone oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
QOR_YEAST
Publication Abstract from PubMed
Quinone oxidoreductase (QOR EC1.6.5.5) catalyzes the reduction of quinone to hydroxyquinone using NADPH as a cofactor. Here we present the crystal structure of the zeta-crystallin-like QOR Zta1 from Saccharomycescerevisiae in apo-form at 2.00 A and complexed with NADPH at 1.59 A resolution. Zta1 forms a homodimer, with each subunit containing a catalytic and a cofactor-binding domain. Upon NADPH binding to the interdomain cleft, the two domains shift towards each other, producing a better fit for NADPH, and tightening substrate binding. Computational simulation combined with site-directed mutagenesis and enzymatic activity analysis defined a potential quinone-binding site that determines the stringent substrate specificity. Moreover, multiple-sequence alignment and kinetics assays implied that a single-residue change from Arg in lower organisms to Gly in vertebrates possibly resulted in elevation of enzymatic activity of zeta-crystallin-like QORs throughout evolution.
Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1.,Guo PC, Ma XX, Bao ZZ, Ma JD, Chen Y, Zhou CZ J Struct Biol. 2011 Oct;176(1):112-8. Epub 2011 Jul 26. PMID:21820057[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo PC, Ma XX, Bao ZZ, Ma JD, Chen Y, Zhou CZ. Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1. J Struct Biol. 2011 Oct;176(1):112-8. Epub 2011 Jul 26. PMID:21820057 doi:10.1016/j.jsb.2011.07.010
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