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[[Image:1dms.gif|left|200px]]<br />
<applet load="1dms" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dms, resolution 1.88&Aring;" />
'''STRUCTURE OF DMSO REDUCTASE'''<br />


==Overview==
==STRUCTURE OF DMSO REDUCTASE==
The periplasmic dimethyl sulfoxide reductase (DMSOR) from the, photosynthetic purple bacterium Rhodobacter capsulatus functions as the, terminal electron acceptor in its respiratory chain. The enzyme catalyzes, the reduction of highly oxidized substrates like dimethyl sulfoxide to, dimethyl sulfide. At a molybdenum redox center, two single electrons are, transferred from cytochrome C556 to the substrate dimethyl sulfoxide, generating dimethyl sulfide and (with two protons) water. The enzyme was, purified and crystallized in space group P4(1)2(1)2 with unit cell, dimensions of a = b = 80.7 A and c = 229.2 A. The crystals diffract beyond, 1.8 A with synchrotron radiation. The three-dimensional structure was, solved by a combination of multiple isomorphous replacement and molecular, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8890912 (full description)]]
<StructureSection load='1dms' size='340' side='right'caption='[[1dms]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1dms]] 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=1DMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DMS FirstGlance]. <br>
1DMS 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 PGD and MM4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: MOL and PGD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DMS OCA]].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MO:MOLYBDENUM+(IV)OXIDE'>2MO</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>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dms OCA], [https://pdbe.org/1dms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dms RCSB], [https://www.ebi.ac.uk/pdbsum/1dms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dms ProSAT]</span></td></tr>
Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution., Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein J, J Mol Biol. 1996 Oct 18;263(1):53-69. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8890912 8890912]
</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/dm/1dms_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=1dms ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodobacter capsulatus]]
[[Category: Rhodobacter capsulatus]]
[[Category: Single protein]]
[[Category: Huber R]]
[[Category: Huber, R.]]
[[Category: Kisker C]]
[[Category: Kisker, C.]]
[[Category: Knaeblein J]]
[[Category: Knaeblein, J.]]
[[Category: Loewe J]]
[[Category: Loewe, J.]]
[[Category: Schindelin H]]
[[Category: Schindelin, H.]]
[[Category: Schneider F]]
[[Category: Schneider, F.]]
[[Category: MM4]]
[[Category: PGD]]
[[Category: dmso reductase]]
[[Category: molydopterin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:01:28 2007''

Latest revision as of 09:56, 7 February 2024

STRUCTURE OF DMSO REDUCTASESTRUCTURE OF DMSO REDUCTASE

Structural highlights

1dms is a 1 chain structure with sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.88Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ McEwan AG, Ferguson SJ, Jackson JB. Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme. Biochem J. 1991 Feb 15;274 ( Pt 1):305-7. PMID:2001248
  2. ↑ Shaw AL, Hanson GR, McEwan AG. Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus. Biochim Biophys Acta. 1996 Sep 30;1276(3):176-80. PMID:8856102

1dms, resolution 1.88Å

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