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| | <StructureSection load='2o4u' size='340' side='right'caption='[[2o4u]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2o4u' size='340' side='right'caption='[[2o4u]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2o4u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crab-eating_macaque Crab-eating macaque]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O4U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2o4u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Macaca_fascicularis Macaca fascicularis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O4U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ofg|1ofg]], [[2glx|2glx]], [[2o48|2o48]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trans-1,2-dihydrobenzene-1,2-diol_dehydrogenase Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.20 1.3.1.20] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o4u OCA], [https://pdbe.org/2o4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o4u RCSB], [https://www.ebi.ac.uk/pdbsum/2o4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o4u ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o4u OCA], [https://pdbe.org/2o4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o4u RCSB], [https://www.ebi.ac.uk/pdbsum/2o4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o4u ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DHDH_MACFA DHDH_MACFA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Crab-eating macaque]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase]] | + | [[Category: Macaca fascicularis]] |
| - | [[Category: Carbone, V]] | + | [[Category: Carbone V]] |
| - | [[Category: El-Kabbani, O]] | + | [[Category: El-Kabbani O]] |
| - | [[Category: Nadp-binding rossmann-fold domain]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Predominantly anti-parallel beta sheet]]
| + | |
| Structural highlights
Function
DHDH_MACFA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carbone V, Endo S, Sumii R, Chung RP, 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. 2008 Jan 1;70(1):176-87. PMID:17654552 doi:10.1002/prot.21566
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