2o48: Difference between revisions

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[[Image:2o48.jpg|left|200px]]


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==Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase==
The line below this paragraph, containing "STRUCTURE_2o48", creates the "Structure Box" on the page.
<StructureSection load='2o48' size='340' side='right'caption='[[2o48]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2o48]] 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=2O48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O48 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AC6:P-HYDROXYACETOPHENONE'>AC6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_2o48| PDB=2o48  | SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o48 OCA], [https://pdbe.org/2o48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o48 RCSB], [https://www.ebi.ac.uk/pdbsum/2o48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o48 ProSAT]</span></td></tr>
 
</table>
'''Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase'''
== Function ==
 
[https://www.uniprot.org/uniprot/DHDH_MACFA DHDH_MACFA]
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o4/2o48_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=2o48 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.
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==
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>
2O48 is a [[Single protein]] structure of 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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://www.ncbi.nlm.nih.gov/pubmed/17654552 17654552]
</div>
<div class="pdbe-citations 2o48" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Macaca fascicularis]]
[[Category: Macaca fascicularis]]
[[Category: Single protein]]
[[Category: Carbone V]]
[[Category: Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase]]
[[Category: El-Kabbani O]]
[[Category: Carbone, V.]]
[[Category: El-Kabbani, O.]]
[[Category: Nadp-binding rossmann-fold domain]]
[[Category: Oxidoreductase]]
[[Category: Predominantly anti-parallel beta sheet]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:18:23 2008''

Latest revision as of 00:14, 28 December 2023

Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase

2o48, resolution 2.59Å

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