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1eu1

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==THE CRYSTAL STRUCTURE OF RHODOBACTER SPHAEROIDES DIMETHYLSULFOXIDE REDUCTASE REVEALS TWO DISTINCT MOLYBDENUM COORDINATION ENVIRONMENTS.==
==THE CRYSTAL STRUCTURE OF RHODOBACTER SPHAEROIDES DIMETHYLSULFOXIDE REDUCTASE REVEALS TWO DISTINCT MOLYBDENUM COORDINATION ENVIRONMENTS.==
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<StructureSection load='1eu1' size='340' side='right' caption='[[1eu1]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='1eu1' size='340' side='right'caption='[[1eu1]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1eu1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cxt 1cxt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EU1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1eu1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cxs 1cxs] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cxt 1cxt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EU1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6MO:MOLYBDENUM(VI)+ION'>6MO</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></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=6MO:MOLYBDENUM(VI)+ION'>6MO</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cxs|1cxs]], [[1cxt|1cxt]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eu1 OCA], [https://pdbe.org/1eu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eu1 RCSB], [https://www.ebi.ac.uk/pdbsum/1eu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eu1 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eu1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eu1 RCSB], [http://www.ebi.ac.uk/pdbsum/1eu1 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DMSA_RHOSH DMSA_RHOSH]] 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:9401017</ref>
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[https://www.uniprot.org/uniprot/DSTOR_CERSP DSTOR_CERSP] 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:9401017</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eu/1eu1_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eu/1eu1_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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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</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=1eu1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Rhodococcus capsulatus molisch 1907]]
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[[Category: Cereibacter sphaeroides]]
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[[Category: Li, H K]]
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[[Category: Large Structures]]
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[[Category: Rajagopalan, K V]]
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[[Category: Li HK]]
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[[Category: Schindelin, H]]
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[[Category: Rajagopalan KV]]
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[[Category: Temple, K]]
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[[Category: Schindelin H]]
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[[Category: Dmso]]
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[[Category: Temple K]]
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[[Category: Mgd]]
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[[Category: Molybdenum]]
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[[Category: Molybdenum cofactor]]
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[[Category: Molybdopterin]]
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[[Category: Oxidoreductase]]
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[[Category: Reductase]]
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Current revision

THE CRYSTAL STRUCTURE OF RHODOBACTER SPHAEROIDES DIMETHYLSULFOXIDE REDUCTASE REVEALS TWO DISTINCT MOLYBDENUM COORDINATION ENVIRONMENTS.

PDB ID 1eu1

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