2C1X

Structure and activity of a flavonoid 3-O glucosyltransferase reveals the basis for plant natural product modification

2C1X の概要

• エントリーDOI: 10.2210/pdb2c1x/pdb
• 関連するPDBエントリー: 2C1Z 2C9Z
• 分子名称: UDP-GLUCOSE FLAVONOID 3-O GLYCOSYLTRANSFERASE, URIDINE-5'-DIPHOSPHATE, 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, flavonoid, wine, catalysis, glycosylation, transferase
• 由来する生物種: VITIS VINIFERA (GRAPE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50874.90

構造登録者

Offen, W.,Martinez-Fleites, C.,Kiat-Lim, E.,Yang, M.,Davis, B.G.,Tarling, C.A.,Ford, C.M.,Bowles, D.J.,Davies, G.J. (登録日: 2005-09-22, 公開日: 2006-01-09, 最終更新日: 2024-05-08)

主引用文献

Offen, W.,Martinez-Fleites, C.,Yang, M.,Kiat-Lim, E.,Davis, B.G.,Tarling, C.A.,Ford, C.M.,Bowles, D.J.,Davies, G.J.
Structure of a Flavonoid Glucosyltransferase Reveals the Basis for Plant Natural Product Modification.
Embo J., 25:1396-, 2006

PubMed Abstract: Glycosylation is a key mechanism for orchestrating the bioactivity, metabolism and location of small molecules in living cells. In plants, a large multigene family of glycosyltransferases is involved in these processes, conjugating hormones, secondary metabolites, biotic and abiotic environmental toxins, to impact directly on cellular homeostasis. The red grape enzyme UDP-glucose:flavonoid 3-O-glycosyltransferase (VvGT1) is responsible for the formation of anthocyanins, the health-promoting compounds which, in planta, function as colourants determining flower and fruit colour and are precursors for the formation of pigmented polymers in red wine. We show that VvGT1 is active, in vitro, on a range of flavonoids. VvGT1 is somewhat promiscuous with respect to donor sugar specificity as dissected through full kinetics on a panel of nine sugar donors. The three-dimensional structure of VvGT1 has also been determined, both in its 'Michaelis' complex with a UDP-glucose-derived donor and the acceptor kaempferol and in complex with UDP and quercetin. These structures, in tandem with kinetic dissection of activity, provide the foundation for understanding the mechanism of these enzymes in small molecule homeostasis.

PubMed: 16482224
DOI: 10.1038/SJ.EMBOJ.7600970

実験手法

X-RAY DIFFRACTION (1.9 Å)