1gp5: Difference between revisions

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[[Image:1gp5.png|left|200px]]


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==Anthocyanidin synthase from Arabidopsis thaliana complexed with trans-dihydroquercetin==
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<StructureSection load='1gp5' size='340' side='right'caption='[[1gp5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gp5]] 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=1GP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GP5 FirstGlance]. <br>
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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]] 2.2&#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=DH2:(2S,3S)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE'>DH2</scene>, <scene name='pdbligand=DQH:(2R,3R)-2-(3,4-DIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE'>DQH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
{{STRUCTURE_1gp5|  PDB=1gp5  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp5 OCA], [https://pdbe.org/1gp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gp5 RCSB], [https://www.ebi.ac.uk/pdbsum/1gp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gp5 ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/1gp5_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=1gp5 ConSurf].
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== Publication Abstract from PubMed ==
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.


===ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN===
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 11796114 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_11796114}}
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</StructureSection>
==About this Structure==
1GP5 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=1GP5 OCA].
 
==Reference==
<ref group="xtra">PMID:11796114</ref><ref group="xtra">PMID:11223521</ref><ref group="xtra">PMID:10074715</ref><references group="xtra"/>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Leucocyanidin oxygenase]]
[[Category: Large Structures]]
[[Category: Clifton, I J.]]
[[Category: Clifton IJ]]
[[Category: Prescott, A G.]]
[[Category: Prescott AG]]
[[Category: Schofield, C J.]]
[[Category: Schofield CJ]]
[[Category: Turnbull, J J.]]
[[Category: Turnbull JJ]]
[[Category: Welford, R W.D.]]
[[Category: Welford RWD]]
[[Category: Wilmouth, R C.]]
[[Category: Wilmouth RC]]
[[Category: 2-oxoglutarate dependent dioxygenase]]
[[Category: Dioxygenase]]
[[Category: Flavonoid biosynthesis]]
[[Category: Oxidoreductase]]
 
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