2c1x: Difference between revisions
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[[Image:2c1x.gif|left|200px]]<br /><applet load="2c1x" size=" | [[Image:2c1x.gif|left|200px]]<br /><applet load="2c1x" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2c1x, resolution 1.90Å" /> | caption="2c1x, resolution 1.90Å" /> | ||
'''STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL PRODUCT MODIFICATION'''<br /> | '''STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL PRODUCT MODIFICATION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2C1X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vitis_vinifera Vitis vinifera] with UDP and B3P as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Flavonol_3-O-glucosyltransferase Flavonol 3-O-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.91 2.4.1.91] Known structural/functional Site: <scene name='pdbsite=AC1:B3p Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 2C1X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vitis_vinifera Vitis vinifera] with <scene name='pdbligand=UDP:'>UDP</scene> and <scene name='pdbligand=B3P:'>B3P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Flavonol_3-O-glucosyltransferase Flavonol 3-O-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.91 2.4.1.91] Known structural/functional Site: <scene name='pdbsite=AC1:B3p+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1X OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: wine]] | [[Category: wine]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:30:26 2008'' | ||
Revision as of 11:30, 3 February 2008
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STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL PRODUCT MODIFICATION
OverviewOverview
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.
About this StructureAbout this Structure
2C1X is a Single protein structure of sequence from Vitis vinifera with and as ligands. Active as Flavonol 3-O-glucosyltransferase, with EC number 2.4.1.91 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
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