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| | <StructureSection load='3c1t' size='340' side='right'caption='[[3c1t]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='3c1t' size='340' side='right'caption='[[3c1t]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3c1t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Grape Grape]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C1T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3c1t]] is a 4 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=3C1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C1T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYC:3,5,7-TRIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-4H-CHROMEN-4-ONE'>MYC</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.252Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2iod|2iod]], [[3bxx|3bxx]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYC:3,5,7-TRIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-4H-CHROMEN-4-ONE'>MYC</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DFR1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29760 Grape])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrokaempferol_4-reductase Dihydrokaempferol 4-reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.219 1.1.1.219] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1t OCA], [https://pdbe.org/3c1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c1t RCSB], [https://www.ebi.ac.uk/pdbsum/3c1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1t ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1t OCA], [https://pdbe.org/3c1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c1t RCSB], [https://www.ebi.ac.uk/pdbsum/3c1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DFRA_VITVI DFRA_VITVI] Bifunctional enzyme involved in flavonoid metabolism.[UniProtKB:Q9XES5] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dihydrokaempferol 4-reductase]] | |
| - | [[Category: Grape]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Delrot, S]] | + | [[Category: Vitis vinifera]] |
| - | [[Category: Estaintot, B Langlois d]] | + | [[Category: Delrot S]] |
| - | [[Category: Gallois, B]] | + | [[Category: Gallois B]] |
| - | [[Category: Granier, T]] | + | [[Category: Granier T]] |
| - | [[Category: Petit, P]] | + | [[Category: Langlois d'Estaintot B]] |
| - | [[Category: Trabelsi, N]] | + | [[Category: Petit P]] |
| - | [[Category: Flavonoid]] | + | [[Category: Trabelsi N]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Short chain dehydrogenase reductase]]
| + | |
| Structural highlights
Function
DFRA_VITVI Bifunctional enzyme involved in flavonoid metabolism.[UniProtKB:Q9XES5]
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
Dihydroflavonol 4-reductase (DFR) is a key enzyme of the flavonoid biosynthesis pathway which catalyses the NADPH-dependent reduction of 2R,3R-trans-dihydroflavonols to leucoanthocyanidins. The latter are the precursors of anthocyans and condensed tannins, two major classes of phenolic compounds that strongly influence the organoleptic properties of wine. DFR has been investigated in many plant species, but little was known about its structural properties until the three-dimensional structure of the Vitis vinifera enzyme complexed with NADP(+) and its natural substrate dihydroquercetin (DHQ) was described. In the course of the study of substrate specificity, crystals of DFR-NADP(+)-flavonol (myricetin and quercetin) complexes were obtained. Their structures exhibit major changes with respect to that of the abortive DFR-NADP(+)-DHQ complex. Two flavonol molecules bind to the catalytic site in a stacking arrangement and alter its geometry, which becomes incompatible with enzymatic activity. The X-ray structures of both DFR-NADP(+)-myricetin and DFR-NADP(+)-quercetin are reported together with preliminary spectroscopic data. The results suggest that flavonols could be inhibitors of the activity of DFR towards dihydroflavonols.
Structural evidence for the inhibition of grape dihydroflavonol 4-reductase by flavonols.,Trabelsi N, Petit P, Manigand C, Langlois d'Estaintot B, Granier T, Chaudiere J, Gallois B Acta Crystallogr D Biol Crystallogr. 2008 Aug;D64(Pt 8):883-91. Epub 2008, Jul 17. PMID:18645237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Trabelsi N, Petit P, Manigand C, Langlois d'Estaintot B, Granier T, Chaudiere J, Gallois B. Structural evidence for the inhibition of grape dihydroflavonol 4-reductase by flavonols. Acta Crystallogr D Biol Crystallogr. 2008 Aug;D64(Pt 8):883-91. Epub 2008, Jul 17. PMID:18645237 doi:10.1107/S0907444908017769
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