2c9z

Structure and activity of a flavonoid 3-0 glucosyltransferase reveals the basis for plant natural product modification

spinqualitylabelsall models 2c9z, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c9z is a 1 chain structure with sequence from Grape. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: QUE, UDP Related: 2c1x, 2c1z Activity: Flavonol 3-O-glucosyltransferase, with EC number 2.4.1.91 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [UFOG_VITVI] In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments. Involved in the formation of red wine pigments. Can use UDP-Glc, UDP-5SGlc, UDP-Xyl, UDP-Man, UDP-Gal, UDP-GlcNAc, GDP-Glc, dTDP-Glc and dTDP-Xyl as sugar donor, but not UDP-6OMeGal, UDP-Ara, UDP-6FGal, UDP-GlcN, UDP-2FGal, UDP-5SAra, GDP-Man, GDPFuc, UDP-Fuc or UDP-Rha. Cyanidin is the natural acceptor, but quercitin and kaempferol can also be glucosylated. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification.,Offen W, Martinez-Fleites C, Yang M, Kiat-Lim E, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ EMBO J. 2006 Mar 22;25(6):1396-405. Epub 2006 Feb 16. PMID:16482224 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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