Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.) |
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Authors: | Shao Hui Dixon Richard A Wang Xiaoqiang |
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Affiliation: | Plant Biology Division, Samuel Roberts Noble Foundation, 2510 Sam Noble Parkway, Ardmore, OK 73401, USA. |
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Abstract: | 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. |
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Keywords: | VR, vestitone reductase rmsd, root-mean-square deviation SDR, short-chain dehydrogenase/reductase SOR, sorphorol reductase IFR, isoflavone reductase DFR, dihydroflavonol reductase ANR, anthocyanidin reductase 17β-HSD1, 17β-hydroxysteroid dehydrogenase type 1 MLCR, mouse lung carbonyl reductase |
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