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[[Image:1e18.gif|left|200px]]<br /><applet load="1e18" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1e18, resolution 2.0&Aring;" />
'''TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS'''<br />


==Overview==
==TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS==
DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as, a molybdoenzyme, will bind tungsten. Protein crystallography has shown, that tungsten in W-DMSOR is ligated by the dithiolene group of the two, pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is, located in a very similar site to that of molybdenum in Mo-DMSOR. These, conclusions are consistent with W L(III)-edge X-ray absorption, EPR and, UV/visible spectroscopic data. W-DMSOR is significantly more active than, Mo-DMSOR in catalysing the reduction of DMSO but, in contrast to the, latter, shows no significant ability to catalyse the oxidation of DMS.
<StructureSection load='1e18' size='340' side='right'caption='[[1e18]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e18]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E18 FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6WO:OXO-TUNGSTEN(VI)'>6WO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=PGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>PGD</scene></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=1e18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e18 OCA], [https://pdbe.org/1e18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e18 RCSB], [https://www.ebi.ac.uk/pdbsum/1e18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e18 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DSTOR_RHOCA DSTOR_RHOCA] Catalyzes the reduction of dimethyl sulfoxide (DMSO) and trimethylamine N-oxide (TMAO) to dimethyl sulfide (DMS) and trimethylamine, respectively. The terminal DMSO reductase can also use various sulfoxides and N-oxide compounds as terminal electron acceptor in addition to DMSO and TMAO.<ref>PMID:2001248</ref> <ref>PMID:8856102</ref>
== Evolutionary Conservation ==
[[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/e1/1e18_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1e18 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will bind tungsten. Protein crystallography has shown that tungsten in W-DMSOR is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-DMSOR. These conclusions are consistent with W L(III)-edge X-ray absorption, EPR and UV/visible spectroscopic data. W-DMSOR is significantly more active than Mo-DMSOR in catalysing the reduction of DMSO but, in contrast to the latter, shows no significant ability to catalyse the oxidation of DMS.


==About this Structure==
Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site.,Stewart LJ, Bailey S, Bennett B, Charnock JM, Garner CD, McAlpine AS J Mol Biol. 2000 Jun 9;299(3):593-600. PMID:10835270<ref>PMID:10835270</ref>
1E18 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with <scene name='pdbligand=PGD:'>PGD</scene>, <scene name='pdbligand=6WO:'>6WO</scene> and <scene name='pdbligand=EOH:'>EOH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=ACT:Active+Site'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E18 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site., Stewart LJ, Bailey S, Bennett B, Charnock JM, Garner CD, McAlpine AS, J Mol Biol. 2000 Jun 9;299(3):593-600. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10835270 10835270]
</div>
<div class="pdbe-citations 1e18" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodobacter capsulatus]]
[[Category: Rhodobacter capsulatus]]
[[Category: Single protein]]
[[Category: Bailey S]]
[[Category: Bailey, S.]]
[[Category: Stewart LJ]]
[[Category: Stewart, L.J.]]
[[Category: 6WO]]
[[Category: EOH]]
[[Category: PGD]]
[[Category: dmso]]
[[Category: molybdenum]]
[[Category: molybdopterin]]
[[Category: oxidoreductase]]
[[Category: reductase]]
[[Category: tungsten]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:36:30 2008''

Latest revision as of 16:58, 8 September 2026

TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

1e18, resolution 2.00Å

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