2c9z

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[[Image:2c9z.gif|left|200px]]<br />
 
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<applet load="2c9z" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2c9z, resolution 2.10&Aring;" />
 
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'''STRUCTURE AND ACTIVITY OF A FLAVONOID 3-0 GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL PRODUCT MODIFICATION'''<br />
 
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==Overview==
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==Structure and activity of a flavonoid 3-0 glucosyltransferase reveals the basis for plant natural product modification==
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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.
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<StructureSection load='2c9z' size='340' side='right'caption='[[2c9z]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c9z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vitis_vinifera Vitis vinifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9Z FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QUE:3,5,7,3,4-PENTAHYDROXYFLAVONE'>QUE</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9z OCA], [https://pdbe.org/2c9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9z RCSB], [https://www.ebi.ac.uk/pdbsum/2c9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UFOG_VITVI 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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9z_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c9z ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:16482224</ref>
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2C9Z 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 QUE 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C9Z OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16482224 16482224]
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</div>
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[[Category: Flavonol 3-O-glucosyltransferase]]
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<div class="pdbe-citations 2c9z" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Vitis vinifera]]
[[Category: Vitis vinifera]]
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[[Category: Bowles, D.J.]]
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[[Category: Bowles DJ]]
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[[Category: Davies, G.J.]]
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[[Category: Davies GJ]]
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[[Category: Davis, B.G.]]
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[[Category: Davis BG]]
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[[Category: Ford, C.M.]]
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[[Category: Ford CM]]
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[[Category: Kiat-Lim, E.]]
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[[Category: Kiat-Lim E]]
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[[Category: Martinez-Fleites, C.]]
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[[Category: Martinez-Fleites C]]
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[[Category: Offen, W.]]
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[[Category: Offen W]]
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[[Category: Tarling, C.A.]]
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[[Category: Tarling CA]]
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[[Category: Yang, M.]]
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[[Category: Yang M]]
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[[Category: QUE]]
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[[Category: UDP]]
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[[Category: catalysis]]
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[[Category: flavonoid]]
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[[Category: glycosylation]]
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[[Category: glycosyltransferase]]
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[[Category: transferase]]
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[[Category: wine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:26:17 2007''
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Current revision

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

PDB ID 2c9z

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