View source for 3hfs


==Structure of apo anthocyanidin reductase from vitis vinifera==
<StructureSection load='3hfs' size='340' side='right'caption='[[3hfs]], [[Resolution|resolution]] 3.17&Aring;' 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]] 3.17&#8491;</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].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== 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]]