2c1x
From Proteopedia
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- | [[Image:2c1x.gif|left|200px]] | + | [[Image:2c1x.gif|left|200px]] |
- | + | ||
- | '''STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL PRODUCT MODIFICATION''' | + | {{Structure |
+ | |PDB= 2c1x |SIZE=350|CAPTION= <scene name='initialview01'>2c1x</scene>, resolution 1.90Å | ||
+ | |SITE= <scene name='pdbsite=AC1:B3p+Binding+Site+For+Chain+A'>AC1</scene> | ||
+ | |LIGAND= <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene> and <scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene> | ||
+ | |ACTIVITY= [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] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL PRODUCT MODIFICATION''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2C1X is a [ | + | 2C1X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vitis_vinifera Vitis vinifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1X OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16482224 16482224] |
[[Category: Flavonol 3-O-glucosyltransferase]] | [[Category: Flavonol 3-O-glucosyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: wine]] | [[Category: wine]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:09:46 2008'' |
Revision as of 14:09, 20 March 2008
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, resolution 1.90Å | |||||||
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Sites: | |||||||
Ligands: | and | ||||||
Activity: | Flavonol 3-O-glucosyltransferase, with EC number 2.4.1.91 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL PRODUCT MODIFICATION
Overview
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 Structure
2C1X is a Single protein structure of sequence from Vitis vinifera. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 16:09:46 2008
Categories: Flavonol 3-O-glucosyltransferase | Single protein | Vitis vinifera | Bowles, D J. | Davies, G J. | Davis, B G. | Ford, C M. | Kiat-Lim, E. | Martinez-Fleites, C. | Offen, W. | Tarling, C A. | Yang, M. | B3P | UDP | Catalysis | Flavonoid | Glycosylation | Glycosyltransferase | Transferase | Wine