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2o48
From Proteopedia
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| - | [[Image:2o48.jpg|left|200px]] | + | [[Image:2o48.jpg|left|200px]] |
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| - | '''Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase''' | + | {{Structure |
| + | |PDB= 2o48 |SIZE=350|CAPTION= <scene name='initialview01'>2o48</scene>, resolution 2.59Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=AC6:P-HYDROXYACETOPHENONE'>AC6</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2O48 is a [ | + | 2O48 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=2O48 OCA]. |
==Reference== | ==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:[http:// | + | 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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:54:51 2008'' |
Revision as of 15:54, 20 March 2008
| |||||||
| , resolution 2.59Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
2O48 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
Page seeded by OCA on Thu Mar 20 17:54:51 2008
