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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''' | '''Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase''' | ||
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[[Category: Carbone, V.]] | [[Category: Carbone, V.]] | ||
[[Category: El-Kabbani, O.]] | [[Category: El-Kabbani, O.]] | ||
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| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Predominantly anti-parallel beta sheet]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:18:23 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:18, 4 May 2008
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 Sun May 4 10:18:23 2008
