3qwa
From Proteopedia
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- | [[ | + | ==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=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3qwa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qwb|3qwb]]</td></tr> | ||
+ | <tr><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=4932 Saccharomyces cerevisiae])</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=3qwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qwa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qwa RCSB], [http://www.ebi.ac.uk/pdbsum/3qwa PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:21820057</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: NADPH:quinone reductase]] | [[Category: NADPH:quinone reductase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] |
Revision as of 04:44, 5 June 2014
Crystal structure of Saccharomyces cerevisiae Zeta-crystallin-like quinone oxidoreductase Zta1
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