2C29

Structure of dihydroflavonol reductase from Vitis vinifera at 1.8 A.

Summary for 2C29

• Entry DOI: 10.2210/pdb2c29/pdb
• Descriptor: DIHYDROFLAVONOL 4-REDUCTASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, (2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE, ... (4 entities in total)
• Functional Keywords: flavonoids, short dehydrogenase reductase, nadph, dihydroquercetin, rossmann fold, oxidoreductase
• Biological source: VITIS VINIFERA (GRAPE)
• Total number of polymer chains: 2
• Total formula weight: 77484.00

Authors

Petit, P.,Granier, T.,D'Estaintot, B.L.,Hamdi, S.,Gallois, B. (deposition date: 2005-09-27, release date: 2006-10-16, Last modification date: 2024-05-08)

Primary citation

Petit, P.,Granier, T.,D'Estaintot, B.L.,Manigand, C.,Bathany, K.,Schmitter, J.M.,Lauvergeat, V.,Hamdi, S.,Gallois, B.
Crystal Structure of Grape Dihydroflavonol 4-Reductase, a Key Enzyme in Flavonoid Biosynthesis.
J.Mol.Biol., 368:1345-, 2007

PubMed Abstract: The nicotinamide adenine dinucleotide phosphate (NADPH)-dependent enzyme dihydroflavonol 4-reductase (DFR) catalyzes a late step in the biosynthesis of anthocyanins and condensed tannins, two flavonoid classes of importance to plant survival and human nutrition. This enzyme has been widely investigated in many plant species, but little is known about its structural and biochemical properties. To provide a basis for detailed structure-function studies, the crystal structure of Vitis vinifera DFR, heterologously expressed in Escherichia coli, has been determined at 1.8 A resolution. The 3D structure of the ternary complex obtained with the oxidized form of nicotinamide adenine dinucleotide phosphate and dihydroquercetin, one of the DFR substrates, presents common features with the short-chain dehydrogenase/reductase family, i.e., an N-terminal domain adopting a Rossmann fold and a variable C-terminal domain, which participates in substrate binding. The structure confirms the importance of the 131-156 region, which lines the substrate binding site and enlightens the role of a specific residue at position 133 (Asn or Asp), assumed to control substrate recognition. The activity of the wild-type enzyme and its variant N133D has been quantified in vitro, using dihydroquercetin or dihydrokaempferol. Our results demonstrate that position 133 cannot be solely responsible for the recognition of the B-ring hydroxylation pattern of dihydroflavonols.

PubMed: 17395203
DOI: 10.1016/J.JMB.2007.02.088

Experimental method

X-RAY DIFFRACTION (1.81 Å)