2c54

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Revision as of 21:47, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2c54" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c54, resolution 1.500Å" /> '''GDP-MANNOSE-3', 5'...)
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File:2c54.gif


2c54, resolution 1.500Å

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GDP-MANNOSE-3', 5'-EPIMERASE (ARABIDOPSIS THALIANA), K178R, WITH GDP-BETA-L-GULOSE AND GDP-4-KETO-BETA-L-GULOSE BOUND IN ACTIVE SITE.

OverviewOverview

GDP-mannose-3',5'-epimerase (GME) from Arabidopsis thaliana catalyzes the, epimerization of both the 3' and 5' positions of GDP-alpha-D-mannose to, yield GDP-beta-L-galactose. Production of the C5' epimer of, GDP-alpha-D-mannose, GDP-beta-L-gulose, has also been reported. The, reaction occurs as part of vitamin C biosynthesis in plants. We have, determined structures of complexes of GME with GDP-alpha-D-mannose, GDP-beta-L-galactose, and a mixture of GDP-beta-L-gulose with, GDP-beta-L-4-keto-gulose to resolutions varying from 2.0 to 1.4 A. The, enzyme has the classical extended short-chain dehydratase/reductase (SDR), fold. We have confirmed that GME establishes an equilibrium between two, products, GDP-beta-L-galactose and GDP-beta-L-gulose. The reaction, proceeds by C4' oxidation of ... [(full description)]

About this StructureAbout this Structure

2C54 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with GKE, NAD, EPE and FMT as [ligands]. Active as [[1]], with EC number [5.1.3.18]. Full crystallographic information is available from [OCA].

ReferenceReference

Structure and function of GDP-mannose-3',5'-epimerase: an enzyme which performs three chemical reactions at the same active site., Major LL, Wolucka BA, Naismith JH, J Am Chem Soc. 2005 Dec 28;127(51):18309-20. PMID:16366586

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