This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2c59
From Proteopedia
(New page: 200px<br /> <applet load="2c59" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c59, resolution 2.00Å" /> '''GDP-MANNOSE-3', 5'-...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2C59 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 GDD, 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=2C59 OCA]]. | + | 2C59 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 GDD, 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=2C59 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]] | ||
| + | [[Category: GDP-mannose 3,5-epimerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Major, L.L.]] | [[Category: Major, L.L.]] | ||
| Line 31: | Line 32: | ||
[[Category: vitamin c]] | [[Category: vitamin c]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:36:50 2007'' |
Revision as of 11:32, 30 October 2007
|
GDP-MANNOSE-3', 5'-EPIMERASE (ARABIDOPSIS THALIANA), WITH GDP-ALPHA-D-MANNOSE AND 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
2C59 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with GDD, 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 13:36:50 2007
Categories: Arabidopsis thaliana | GDP-mannose 3,5-epimerase | Single protein | Major, L.L. | Naismith, J.H. | Wolucka, B.A. | BTB | FMT | GDD | NAD | 3' 5'-epimerase | Ascorbate biosynthesis | Gdp-galactose | Gdp-gulose | Gdp-mannose | Isomerase | Keto intermediate | Short chain dehydratase/reductase | Vitamin c
