1gp5: Difference between revisions

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


{{Structure
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The line below this paragraph, containing "STRUCTURE_1gp5", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=IRN:2og+Binding+Site+For+Chain+A'>IRN</scene>
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|ACTIVITY=  
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|GENE=  
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|DOMAIN=
{{STRUCTURE_1gp5| PDB=1gp5  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp5 OCA], [http://www.ebi.ac.uk/pdbsum/1gp5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gp5 RCSB]</span>
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'''ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN'''
'''ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN'''
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[[Category: Wilmouth, R C.]]
[[Category: Wilmouth, R C.]]
[[Category: 2-oxoglutarate dependent dioxygenase]]
[[Category: 2-oxoglutarate dependent dioxygenase]]
[[Category: flavonoid biosynthesis]]
[[Category: Flavonoid biosynthesis]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:50:45 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:37 2008''

Revision as of 17:50, 2 May 2008

File:1gp5.jpg

Template:STRUCTURE 1gp5

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. 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 Page seeded by OCA on Fri May 2 17:50:45 2008

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