2O48
Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase
Summary for 2O48
| Entry DOI | 10.2210/pdb2o48/pdb |
| Related | 1OFG 2GLX |
| Descriptor | Dimeric dihydrodiol dehydrogenase, SULFATE ION, P-HYDROXYACETOPHENONE, ... (5 entities in total) |
| Functional Keywords | nadp-binding rossmann-fold domain, predominantly anti-parallel beta sheet, oxidoreductase |
| Biological source | Macaca fascicularis (crab-eating macaque) |
| Total number of polymer chains | 1 |
| Total formula weight | 37079.56 |
| Authors | Carbone, V.,El-Kabbani, O. (deposition date: 2006-12-04, release date: 2007-07-31, Last modification date: 2023-12-27) |
| Primary citation | Carbone, V.,Endo, S.,Sumii, R.,Chung, R.P.,Matsunaga, T.,Hara, A.,El-Kabbani, O. Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis. Proteins, 70:176-187, 2008 Cited by PubMed Abstract: 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. PubMed: 17654552DOI: 10.1002/prot.21566 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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