View source for 3qwa


==Crystal structure of Saccharomyces cerevisiae Zeta-crystallin-like quinone oxidoreductase Zta1==
<StructureSection load='3qwa' size='340' side='right'caption='[[3qwa]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/QOR_YEAST QOR_YEAST] 
<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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qwa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Bao ZZ]]
[[Category: Chen YX]]
[[Category: Guo PC]]
[[Category: Ma XX]]
[[Category: Zhou CZ]]