2p4h | pdb_00002p4h

Crystal Structure of Vestitone Reductase from Alfalfa (Medicago sativa L.)

spinqualitylabelsall models 2p4h, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2p4h is a 1 chain structure with sequence from Alfalfa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: Vestitone Reductase (Alfalfa) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VESTR_MEDSA] Stereospecific enzyme that catalyzes the NADPH-dependent reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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