2p4h

<table><tr><td colspan='2'>[[2p4h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alfalfa Alfalfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P4H FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vestitone Reductase ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3879 Alfalfa])</td></tr>

[[https://www.uniprot.org/uniprot/VESTR_MEDSA 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.<ref>PMID:7625843</ref> <ref>PMID:7805842</ref> <ref>PMID:8071365</ref>

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== 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<ref>PMID:17433362</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2p4h" style="background-color:#fffaf0;"></div>

[[Category: Alfalfa]]

[[Category: Dixon, R A]]

[[Category: Shao, H]]

[[Category: Wang, X]]

[[Category: Isoflavonoid]]

[[Category: Plant protein]]