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2c54

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[[Image:2c54.gif|left|200px]]
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{{STRUCTURE_2c54| PDB=2c54 | SCENE= }}
{{STRUCTURE_2c54| PDB=2c54 | SCENE= }}
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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.'''
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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.===
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==Overview==
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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 GDP-alpha-D-mannose followed by epimerization of the C5' position to give GDP-beta-L-4-keto-gulose. This intermediate is either reduced to give GDP-beta-L-gulose or the C3' position is epimerized to give GDP-beta-L-4-keto-galactose, then C4' is reduced to GDP-beta-L-galactose. The combination of oxidation, epimerization, and reduction in a single active site is unusual. Structural analysis coupled to site-directed mutagenesis suggests C145 and K217 as the acid/base pair responsible for both epimerizations. On the basis of the structure of the GDP-beta-L-gulose/GDP-beta-L-4-keto-gulose co-complex, we predict that a ring flip occurs during the first epimerization and that a boat intermediate is likely for the second epimerization. Comparison of GME with other SDR enzymes known to abstract a protein alpha to the keto function of a carbohydrate identifies key common features.
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(as it appears on PubMed at http://www.pubmed.gov), where 16366586 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16366586}}
==About this Structure==
==About this Structure==
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[[Category: Short chain dehydratase/reductase]]
[[Category: Short chain dehydratase/reductase]]
[[Category: Vitamin c]]
[[Category: Vitamin c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:15:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:43:39 2008''

Revision as of 17:43, 28 July 2008

Image:2c54.png

Template:STRUCTURE 2c54

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

Template:ABSTRACT PUBMED 16366586

About this Structure

2C54 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 20:43:39 2008

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