2C29

Structure of dihydroflavonol reductase from Vitis vinifera at 1.8 A.

2C29 の概要

• エントリーDOI: 10.2210/pdb2c29/pdb
• 分子名称: 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)
• 機能のキーワード: flavonoids, short dehydrogenase reductase, nadph, dihydroquercetin, rossmann fold, oxidoreductase
• 由来する生物種: VITIS VINIFERA (GRAPE)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77484.00

構造登録者

Petit, P.,Granier, T.,D'Estaintot, B.L.,Hamdi, S.,Gallois, B. (登録日: 2005-09-27, 公開日: 2006-10-16, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.81 Å)