2c1x

From Proteopedia

(Difference between revisions)

Revision as of 08:05, 23 May 2018

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

Structural highlights

2c1x 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:	,
Related:	2c1z, 2c9z
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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Offen W, Martinez-Fleites C, Yang M, Kiat-Lim E, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ. Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO J. 2006 Mar 22;25(6):1396-405. Epub 2006 Feb 16. PMID:16482224

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c1x"

@@ Line 1: / Line 1: @@
-==STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL PRODUCT MODIFICATION==
+==Structure and activity of a flavonoid 3-O glucosyltransferase reveals the basis for plant natural product modification==
 <StructureSection load='2c1x' size='340' side='right' caption='[[2c1x]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c1z|2c1z]], [[2c9z|2c9z]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1x OCA], [http://pdbe.org/2c1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c1x RCSB], [http://www.ebi.ac.uk/pdbsum/2c1x PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1x OCA], [http://pdbe.org/2c1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c1x RCSB], [http://www.ebi.ac.uk/pdbsum/2c1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c1x ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/2c1x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/2c1x_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2c1x

From Proteopedia

Revision as of 08:05, 23 May 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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