2P4H

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

Summary for 2P4H

• Entry DOI: 10.2210/pdb2p4h/pdb
• Descriptor: Vestitone reductase (2 entities in total)
• Functional Keywords: nadph-dependent reductase, isoflavonoid, plant protein
• Biological source: Medicago sativa
• Total number of polymer chains: 1
• Total formula weight: 35571.68

Authors

Wang, X.,Shao, H.,Dixon, R.A. (deposition date: 2007-03-12, release date: 2007-05-15, Last modification date: 2024-02-21)

Primary citation

Shao, H.,Dixon, R.A.,Wang, X.
Crystal Structure of Vestitone Reductase from Alfalfa (Medicago sativa L.).
J.Mol.Biol., 369:265-276, 2007

PubMed 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.

PubMed: 17433362
DOI: 10.1016/j.jmb.2007.03.040

Experimental method

X-RAY DIFFRACTION (1.4 Å)