2o4u

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[[Image:2o4u.jpg|left|200px]]<br /><applet load="2o4u" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2o4u.jpg|left|200px]]
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caption="2o4u, resolution 2.00&Aring;" />
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'''Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase'''<br />
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{{Structure
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|PDB= 2o4u |SIZE=350|CAPTION= <scene name='initialview01'>2o4u</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Trans-1,2-dihydrobenzene-1,2-diol_dehydrogenase Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.20 1.3.1.20]
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|GENE=
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}}
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'''Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2O4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Macaca_fascicularis Macaca fascicularis] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=BME:'>BME</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trans-1,2-dihydrobenzene-1,2-diol_dehydrogenase Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.20 1.3.1.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O4U OCA].
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2O4U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Macaca_fascicularis Macaca fascicularis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O4U OCA].
==Reference==
==Reference==
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Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis., Carbone V, Endo S, Sumii R, Chung RP, Matsunaga T, Hara A, El-Kabbani O, Proteins. 2008 Jan 1;70(1):176-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17654552 17654552]
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Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis., Carbone V, Endo S, Sumii R, Chung RP, Matsunaga T, Hara A, El-Kabbani O, Proteins. 2008 Jan 1;70(1):176-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17654552 17654552]
[[Category: Macaca fascicularis]]
[[Category: Macaca fascicularis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: predominantly anti-parallel beta sheet]]
[[Category: predominantly anti-parallel beta sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:14:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:55:10 2008''

Revision as of 15:55, 20 March 2008


PDB ID 2o4u

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , and
Activity: Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, with EC number 1.3.1.20
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase


Overview

Dimeric dihydrodiol dehydrogenase (DD) catalyses the nicotinamide adenine dinucleotide phosphate (NADP+)-dependent oxidation of trans-dihydrodiols of aromatic hydrocarbons to their corresponding catechols. This is the first report of the crystal structure of the dimeric enzyme determined at 2.0 A resolution. The tertiary structure is formed by a classical dinucleotide binding fold comprising of two betaalphabetaalphabeta motifs at the N-terminus and an eight-stranded, predominantly antiparallel beta-sheet at the C-terminus. The active-site of DD, occupied either by a glycerol molecule or the inhibitor 4-hydroxyacetophenone, is located in the C-terminal domain of the protein and maintained by a number of residues including Lys97, Trp125, Phe154, Leu158, Val161, Asp176, Leu177, Tyr180, Trp254, Phe279, and Asp280. The dimer interface is stabilized by a large number of intermolecular contacts mediated by the beta-sheet of each monomer, which includes an intricate hydrogen bonding network maintained in principal by Arg148 and Arg202. Site-directed mutagenesis has demonstrated that the intact dimer is not essential for catalytic activity. The similarity between the quaternary structures of mammalian DD and glucose-fructose oxidoreductase isolated from the prokaryotic organism Zymomonas mobilis suggests that both enzymes are members of a unique family of oligomeric proteins and may share a common ancestral gene.

About this Structure

2O4U is a Single protein structure of sequence from Macaca fascicularis. Full crystallographic information is available from OCA.

Reference

Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis., Carbone V, Endo S, Sumii R, Chung RP, Matsunaga T, Hara A, El-Kabbani O, Proteins. 2008 Jan 1;70(1):176-87. PMID:17654552

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