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3hfs
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3hfs is ON HOLD Authors: GARGOURI, M., MAUGE, C., LANGLOIS d'ESTAINTOT, B., GRANIER, T., MANIGAN, C., GALLOIS, B. Description: Structure of apo ant...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==Structure of apo anthocyanidin reductase from vitis vinifera== |
| + | <StructureSection load='3hfs' size='340' side='right'caption='[[3hfs]], [[Resolution|resolution]] 3.17Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3hfs]] is a 2 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=3HFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFS FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.17Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=3hfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfs OCA], [https://pdbe.org/3hfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfs RCSB], [https://www.ebi.ac.uk/pdbsum/3hfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANRCS_VITVI ANRCS_VITVI] Produces the terminal flavan-3-ol monomers required for the formation of proanthocyanidins or condensed tannins in leaves and flowers, as well as in the skin and seeds of developing berries (Ref.1, PubMed:16169968). Behaves as a reductase and as a C-3 epimerase (PubMed:20030585). Catalyzes the double reduction of anthocyanidins, producing a mixture of (2S,3S)- and (2S,3R)-flavan-3-ols (Ref.1). The enzyme catalyzes sequential hydride transfers to C-2 and C-4, respectively and epimerization at C-3 is achieved by tautomerization that occurs between the two hydride transfers (PubMed:20030585). Converts cyanidin, pelargonidin and delphinidin into catechin and epicatechin, afzelechin and epiafzelechin, and gallocatechin and epigallocatechin respectively (PubMed:19690377).<ref>PMID:16169968</ref> <ref>PMID:19690377</ref> <ref>PMID:20030585</ref> [UniProtKB:A0A059TC02] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/3hfs_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3hfs ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Together with leucoanthocyanidin reductase, anthocyanidin reductase (ANR) is one of the two enzymes of the flavonoid-biosynthesis pathway that produces the flavan-3-ol monomers required for the formation of proanthocyanidins or condensed tannins. It has been shown to catalyse the double reduction of anthocyanidins to form 2R,3R-flavan-3-ols, which can be further transformed to the 2S,3R isomers by non-enzymatic epimerization. ANR from grape (Vitis vinifera) was expressed in Escherichia coli and purified. Unexpectedly, RP-HPLC, LC-MS and NMR experiments clearly established that the enzyme produces a 50:50 mixture of 2,3-cis and 2,3-trans flavan-3-ols which have been identified by chiral chromatography to be 2S,3S- and 2S,3R-flavan-3-ols, i.e. the naturally rare (+)-epicatechin and (-)-catechin, when cyanidin is used as the substrate of the reaction. The first three-dimensional structure of ANR is described at a resolution of 2.2 A and explains the inactivity of the enzyme in the presence of high salt concentrations. | ||
| - | + | Structure and epimerase activity of anthocyanidin reductase from Vitis vinifera.,Gargouri M, Manigand C, Mauge C, Granier T, Langlois d'Estaintot B, Cala O, Pianet I, Bathany K, Chaudiere J, Gallois B Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):989-1000. Epub 2009, Aug 14. PMID:19690377<ref>PMID:19690377</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3hfs" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Vitis vinifera]] | ||
| + | [[Category: Gallois B]] | ||
| + | [[Category: Gargouri M]] | ||
| + | [[Category: Granier T]] | ||
| + | [[Category: Langlois d'Estaintot B]] | ||
| + | [[Category: Manigan C]] | ||
| + | [[Category: Mauge C]] | ||
Current revision
Structure of apo anthocyanidin reductase from vitis vinifera
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