2o4u
From Proteopedia
(New page: 200px<br /><applet load="2o4u" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o4u, resolution 2.00Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Dimeric dihydrodiol dehydrogenase (DD) catalyses the nicotinamide adenine | + | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: | + | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:14:25 2008'' |
Revision as of 16:14, 21 February 2008
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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
2O4U is a Single protein structure of sequence from Macaca fascicularis with , and as ligands. Active as Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, with EC number 1.3.1.20 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 Feb 21 18:14:25 2008
