1gp5

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(New page: 200px<br /> <applet load="1gp5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gp5, resolution 2.2&Aring;" /> '''ANTHOCYANIDIN SYNTHA...)
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Revision as of 17:40, 29 October 2007

Image:1gp5.gif

1gp5, resolution 2.2Å

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ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN

Overview

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, ... [(full description)]

About this Structure

1GP5 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with FE, AKG, MES, DQH and DH2 as [ligands]. Full crystallographic information is available from [OCA].

Reference

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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