2o48
From Proteopedia
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|PDB= 2o48 |SIZE=350|CAPTION= <scene name='initialview01'>2o48</scene>, resolution 2.59Å | |PDB= 2o48 |SIZE=350|CAPTION= <scene name='initialview01'>2o48</scene>, resolution 2.59Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AC6:P-HYDROXYACETOPHENONE'>AC6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ofg|1OFG]], [[2glx|2GLX]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o48 OCA], [http://www.ebi.ac.uk/pdbsum/2o48 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o48 RCSB]</span> | ||
}} | }} | ||
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[[Category: Carbone, V.]] | [[Category: Carbone, V.]] | ||
[[Category: El-Kabbani, O.]] | [[Category: El-Kabbani, O.]] | ||
| - | [[Category: AC6]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: SO4]] | ||
[[Category: nadp-binding rossmann-fold domain]] | [[Category: nadp-binding rossmann-fold domain]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: predominantly anti-parallel beta sheet]] | [[Category: predominantly anti-parallel beta sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:12:27 2008'' |
Revision as of 01:12, 31 March 2008
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| , resolution 2.59Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, with EC number 1.3.1.20 | ||||||
| Related: | 1OFG, 2GLX
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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