2o48

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[[Image:2o48.png|left|200px]]
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==Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase==
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<StructureSection load='2o48' size='340' side='right' caption='[[2o48]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2o48]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O48 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AC6:P-HYDROXYACETOPHENONE'>AC6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ofg|1ofg]], [[2glx|2glx]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2o48 RCSB], [http://www.ebi.ac.uk/pdbsum/2o48 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o4/2o48_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2o48| PDB=2o48 | SCENE= }}
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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<ref>PMID:17654552</ref>
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===Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_17654552}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2o48]] is a 1 chain structure with 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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:017654552</ref><references group="xtra"/>
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[[Category: Macaca fascicularis]]
[[Category: Macaca fascicularis]]
[[Category: Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase]]
[[Category: Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase]]

Revision as of 19:18, 30 September 2014

Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase

2o48, resolution 2.59Å

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