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1gp4
From Proteopedia
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ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA (SELENOMETHIONINE SUBSTITUTED)
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, 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 Structure
1GP4 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.
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
Page seeded by OCA on Sun Feb 3 09:41:31 2008
