2c5e

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[[Image:2c5e.gif|left|200px]]<br /><applet load="2c5e" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c5e.gif|left|200px]]
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caption="2c5e, resolution 1.700&Aring;" />
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'''GDP-MANNOSE-3', 5'-EPIMERASE (ARABIDOPSIS THALIANA), K217A, WITH GDP-ALPHA-D-MANNOSE BOUND IN THE ACTIVE SITE.'''<br />
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{{Structure
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|PDB= 2c5e |SIZE=350|CAPTION= <scene name='initialview01'>2c5e</scene>, resolution 1.700&Aring;
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|SITE= <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=GDD:GUANOSINE-5'-DIPHOSPHATE-ALPHA-D-MANNOSE'>GDD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''GDP-MANNOSE-3', 5'-EPIMERASE (ARABIDOPSIS THALIANA), K217A, WITH GDP-ALPHA-D-MANNOSE BOUND IN THE ACTIVE SITE.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2C5E 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 <scene name='pdbligand=GDD:'>GDD</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=FMT:'>FMT</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5E OCA].
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2C5E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5E OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/16366586 16366586]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: GDP-mannose 3,5-epimerase]]
[[Category: GDP-mannose 3,5-epimerase]]
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[[Category: vitamin c]]
[[Category: vitamin c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:11:02 2008''

Revision as of 14:11, 20 March 2008

Image:2c5e.gif


PDB ID 2c5e

Drag the structure with the mouse to rotate
, resolution 1.700Å
Sites:
Ligands: , and
Activity: GDP-mannose 3,5-epimerase, with EC number 5.1.3.18
Coordinates: save as pdb, mmCIF, xml



GDP-MANNOSE-3', 5'-EPIMERASE (ARABIDOPSIS THALIANA), K217A, WITH GDP-ALPHA-D-MANNOSE 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 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.

About this Structure

2C5E 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

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