1gp5: Difference between revisions
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[[Image:1gp5.jpg|left|200px]]<br /><applet load="1gp5" size=" | [[Image:1gp5.jpg|left|200px]]<br /><applet load="1gp5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1gp5, resolution 2.2Å" /> | caption="1gp5, resolution 2.2Å" /> | ||
'''ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN'''<br /> | '''ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1GP5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with FE, AKG, MES, DQH and DH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=IRN:2og Binding Site For Chain A'>IRN</scene>. Full crystallographic information is available from [http:// | 1GP5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=AKG:'>AKG</scene>, <scene name='pdbligand=MES:'>MES</scene>, <scene name='pdbligand=DQH:'>DQH</scene> and <scene name='pdbligand=DH2:'>DH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=IRN:2og+Binding+Site+For+Chain+A'>IRN</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GP5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: flavonoid biosynthesis]] | [[Category: flavonoid biosynthesis]] | ||
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Revision as of 10:41, 3 February 2008
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ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN
OverviewOverview
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.
About this StructureAbout this Structure
1GP5 is a Single protein structure of sequence from Arabidopsis thaliana with , , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
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