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2c5a

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(New page: 200px<br /> <applet load="2c5a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c5a, resolution 1.400&Aring;" /> '''GDP-MANNOSE-3', 5'...)
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==About this Structure==
==About this Structure==
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2C5A is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]] with GDC, NAD, BTB and FMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.18 5.1.3.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C5A OCA]].
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2C5A is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]] with GDC, NAD, BTB and FMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/GDP-mannose_3,5-epimerase GDP-mannose 3,5-epimerase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.18 5.1.3.18]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C5A OCA]].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16366586 16366586]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16366586 16366586]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: GDP-mannose 3,5-epimerase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Major, L.L.]]
[[Category: Major, L.L.]]
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[[Category: vitamin c]]
[[Category: vitamin c]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:52:01 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:37:34 2007''

Revision as of 11:32, 30 October 2007


2c5a, resolution 1.400Å

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GDP-MANNOSE-3', 5'-EPIMERASE (ARABIDOPSIS THALIANA), Y174F, WITH GDP-BETA-L-GALACTOSE BOUND IN THE ACTIVE SITE

Overview

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 Structure

2C5A is a [Single protein] structure of sequence from [Arabidopsis thaliana] with GDC, NAD, BTB and FMT as [ligands]. Active as [GDP-mannose 3,5-epimerase], with EC number [5.1.3.18]. Structure known Active Site: AC1. 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 Tue Oct 30 13:37:34 2007

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