1h5q

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[[Image:1h5q.gif|left|200px]]<br /><applet load="1h5q" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h5q.gif|left|200px]]
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caption="1h5q, resolution 1.50&Aring;" />
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'''MANNITOL DEHYDROGENASE FROM AGARICUS BISPORUS'''<br />
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{{Structure
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|PDB= 1h5q |SIZE=350|CAPTION= <scene name='initialview01'>1h5q</scene>, resolution 1.50&Aring;
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|SITE= <scene name='pdbsite=AC1:Ni+Binding+Site+For+Chain+J'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Mannitol_2-dehydrogenase_(NADP(+)) Mannitol 2-dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.138 1.1.1.138]
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|GENE=
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}}
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'''MANNITOL DEHYDROGENASE FROM AGARICUS BISPORUS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1H5Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mannitol_2-dehydrogenase_(NADP(+)) Mannitol 2-dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.138 1.1.1.138] Known structural/functional Site: <scene name='pdbsite=AC1:Ni+Binding+Site+For+Chain+J'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5Q OCA].
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1H5Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5Q OCA].
==Reference==
==Reference==
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The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus., Horer S, Stoop J, Mooibroek H, Baumann U, Sassoon J, J Biol Chem. 2001 Jul 20;276(29):27555-61. Epub 2001 May 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11335726 11335726]
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The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus., Horer S, Stoop J, Mooibroek H, Baumann U, Sassoon J, J Biol Chem. 2001 Jul 20;276(29):27555-61. Epub 2001 May 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11335726 11335726]
[[Category: Agaricus bisporus]]
[[Category: Agaricus bisporus]]
[[Category: Mannitol 2-dehydrogenase (NADP(+))]]
[[Category: Mannitol 2-dehydrogenase (NADP(+))]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:32:37 2008''

Revision as of 09:32, 20 March 2008


PDB ID 1h5q

Drag the structure with the mouse to rotate
, resolution 1.50Å
Sites:
Ligands: and
Activity: Mannitol 2-dehydrogenase (NADP(+)), with EC number 1.1.1.138
Coordinates: save as pdb, mmCIF, xml



MANNITOL DEHYDROGENASE FROM AGARICUS BISPORUS


Overview

Mannitol, an acyclic six-carbon polyol, is one of the most abundant sugar alcohols occurring in nature. In the button mushroom, Agaricus bisporus, it is synthesized from fructose by the enzyme mannitol 2-dehydrogenase (MtDH; EC ) using NADPH as a cofactor. Mannitol serves as the main storage carbon (up to 50% of the fruit body dry weight) and plays a critical role in growth, fruit body development, osmoregulation, and salt tolerance. Furthermore, mannitol dehydrogenases are being evaluated for commercial mannitol production as alternatives to the less efficient chemical reduction of fructose. Given the importance of mannitol metabolism and mannitol dehydrogenases, MtDH was cloned into the pET28 expression system and overexpressed in Escherichia coli. Kinetic and physicochemical properties of the recombinant enzyme are indistinguishable from the natural enzyme. The crystal structure of its binary complex with NADP was solved at 1.5-A resolution and refined to an R value of 19.3%. It shows MtDH to be a tetramer and a member of the short chain dehydrogenase/reductase family of enzymes. The catalytic residues forming the so-called catalytic triad can be assigned to Ser(149), Tyr(169), and Lys(173).

About this Structure

1H5Q is a Single protein structure of sequence from Agaricus bisporus. Full crystallographic information is available from OCA.

Reference

The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus., Horer S, Stoop J, Mooibroek H, Baumann U, Sassoon J, J Biol Chem. 2001 Jul 20;276(29):27555-61. Epub 2001 May 2. PMID:11335726

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