2p4h
From Proteopedia
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Crystal Structure of Vestitone Reductase from Alfalfa (Medicago sativa L.)
Overview
Isoflavonoids are commonly found in leguminous plants, where they play, important roles in plant defense and have significant health benefits for, animals and humans. Vestitone reductase catalyzes a stereospecific, NADPH-dependent reduction of (3R)-vestitone in the biosynthesis of the, antimicrobial isoflavonoid phytoalexin medicarpin. The crystal structure, of alfalfa (Medicago sativa L.) vestitone reductase has been determined at, 1.4 A resolution. The structure contains a classic Rossmann fold domain in, the N terminus and a small C-terminal domain. Sequence and structural, analysis showed that vestitone reductase is a member of the short-chain, dehydrogenase/reductase (SDR) superfamily despite the low levels of, sequence identity, and the prominent structural differences from other SDR, enzymes with known structures. The putative binding sites for the, co-factor NADPH and the substrate (3R)-vestitone were defined and located, in a large cleft formed between the N and C-terminal domains of enzyme., Potential key residues for enzyme activity were also identified, including, the catalytic triad Ser129-Tyr164-Lys168. A molecular docking study showed, that (3R)-vestitone, but not the (3S) isomer, forms favored interactions, with the co-factor and catalytic triad, thus providing an explanation for, the enzyme's strict substrate stereo-specificity.
About this Structure
2P4H is a Single protein structure of sequence from Medicago sativa. Full crystallographic information is available from OCA.
Reference
Crystal Structure of Vestitone Reductase from Alfalfa (Medicago sativa L.)., Shao H, Dixon RA, Wang X, J Mol Biol. 2007 May 25;369(1):265-76. Epub 2007 Mar 21. PMID:17433362
Page seeded by OCA on Wed Jan 23 15:17:19 2008
