1gp4

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{{Seed}}
 
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[[Image:1gp4.png|left|200px]]
 
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==Anthocyanidin synthase from Arabidopsis thaliana (selenomethionine substituted)==
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The line below this paragraph, containing "STRUCTURE_1gp4", creates the "Structure Box" on the page.
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<StructureSection load='1gp4' size='340' side='right'caption='[[1gp4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1gp4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GP4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1gp4| PDB=1gp4 | SCENE= }}
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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=1gp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp4 OCA], [https://pdbe.org/1gp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gp4 RCSB], [https://www.ebi.ac.uk/pdbsum/1gp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gp4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LDOX_ARATH LDOX_ARATH] Involved in anthocyanin and protoanthocyanidin biosynthesis by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins. Possesses low flavonol synthase activity in vitro towards dihydrokaempferol and dihydroquercetin producing kaempferol and quercitin, respectively.<ref>PMID:12940955</ref> <ref>PMID:16153644</ref> <ref>PMID:19433090</ref> <ref>PMID:21683773</ref> <ref>PMID:16106293</ref>
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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/gp/1gp4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1gp4 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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Flavonoids are common colorants in plants and have long-established biomedicinal properties. Anthocyanidin synthase (ANS), a 2-oxoglutarate iron-dependent oxygenase, catalyzes the penultimate step in the biosynthesis of the anthocyanin class of flavonoids. The crystal structure of ANS reveals a multicomponent active site containing metal, cosubstrate, and two molecules of a substrate analog (dihydroquercetin). An additional structure obtained after 30 min exposure to dioxygen is consistent with the oxidation of the dihydroquercetin to quercetin and the concomitant decarboxylation of 2-oxoglutarate to succinate. Together with in vitro studies, the crystal structures suggest a mechanism for ANS-catalyzed anthocyanidin formation from the natural leucoanthocyanidin substrates involving stereoselective C-3 hydroxylation. The structure of ANS provides a template for the ubiquitous family of plant nonhaem oxygenases for future engineering and inhibition studies.
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===ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA (SELENOMETHIONINE SUBSTITUTED)===
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Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana.,Wilmouth RC, Turnbull JJ, Welford RW, Clifton IJ, Prescott AG, Schofield CJ Structure. 2002 Jan;10(1):93-103. PMID:11796114<ref>PMID:11796114</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_11796114}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1gp4" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11796114 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11796114}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1GP4 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GP4 OCA].
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==Reference==
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<ref group="xtra">PMID:11796114</ref><ref group="xtra">PMID:11223521</ref><ref group="xtra">PMID:10074715</ref><references group="xtra"/>
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Clifton, I J.]]
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[[Category: Large Structures]]
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[[Category: Prescott, A G.]]
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[[Category: Clifton IJ]]
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[[Category: Schofield, C J.]]
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[[Category: Prescott AG]]
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[[Category: Turnbull, J J.]]
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[[Category: Schofield CJ]]
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[[Category: Welford, R W.D.]]
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[[Category: Turnbull JJ]]
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[[Category: Wilmouth, R C.]]
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[[Category: Welford RWD]]
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[[Category: 2-oxoglutarate dependent dioxygenase]]
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[[Category: Wilmouth RC]]
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[[Category: Flavonoid biosynthesis]]
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[[Category: Oxygenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 16 20:04:47 2009''
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Current revision

Anthocyanidin synthase from Arabidopsis thaliana (selenomethionine substituted)

PDB ID 1gp4

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