2o48: Difference between revisions
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[[Image:2o48.jpg|left|200px]] | [[Image:2o48.jpg|left|200px]] | ||
'''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
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| 2o48, resolution 2.59Å | |||||||||||||
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| Ligands: | SO4, AC6 and BME | ||||||||||||
| 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
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