4pvd
From Proteopedia
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| - | ''' | + | ==Crystal structure of yeast methylglyoxal/isovaleraldehyde reductase Gre2 complexed with NADPH== |
| + | <StructureSection load='4pvd' size='340' side='right' caption='[[4pvd]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4pvd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PVD FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pvc|4pvc]]</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=4pvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pvd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pvd RCSB], [http://www.ebi.ac.uk/pdbsum/4pvd PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Saccharomyces cerevisiae Gre2 (EC1.1.1.283) serves as a versatile enzyme that catalyzes the stereoselective reduction of a broad range of substrates including aliphatic and aromatic ketones, diketones, as well as aldehydes, using NADPH as the cofactor. Here we present the crystal structures of Gre2 from S. cerevisiae in an apo-form at 2.00A and NADPH-complexed form at 2.40A resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate. Computational simulation combined with site-directed mutagenesis and enzymatic activity analysis enabled us to define a potential substrate-binding pocket that determines the stringent substrate stereoselectivity for catalysis. | ||
| - | + | Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2.,Guo PC, Bao ZZ, Ma XX, Xia Q, Li WF Biochim Biophys Acta. 2014 Sep;1844(9):1486-92. doi:, 10.1016/j.bbapap.2014.05.008. Epub 2014 May 27. PMID:24879127<ref>PMID:24879127</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bao, Z Z.]] | ||
| + | [[Category: Guo, P C.]] | ||
| + | [[Category: Li, W F.]] | ||
| + | [[Category: Zhou, C Z.]] | ||
| + | [[Category: Nadph binding]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Reductase]] | ||
| + | [[Category: Rossmann fold]] | ||
Revision as of 11:43, 22 October 2014
Crystal structure of yeast methylglyoxal/isovaleraldehyde reductase Gre2 complexed with NADPH
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