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{{Seed}}
[[Image:1tmo.png|left|200px]]


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==TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA==
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<StructureSection load='1tmo' size='340' side='right'caption='[[1tmo]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1tmo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_massilia Shewanella massilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TMO 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]] 2.5&#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=2MD:GUANYLATE-O-PHOSPHORIC+ACID+MONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,5,6,7,8A,9,10,10A-OCTAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)+ESTER'>2MD</scene>, <scene name='pdbligand=2MO:MOLYBDENUM+(IV)OXIDE'>2MO</scene></td></tr>
{{STRUCTURE_1tmo|  PDB=1tmo  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tmo OCA], [https://pdbe.org/1tmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tmo RCSB], [https://www.ebi.ac.uk/pdbsum/1tmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tmo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TORA_SHEMA TORA_SHEMA] Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.
== 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/tm/1tmo_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=1tmo ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The periplasmic trimethylamine N-oxide (TMAO) reductase from the marine bacteria Shewanella massilia is involved in a respiratory chain, having trimethylamine N-oxide as terminal electron acceptor. This molybdoenzyme belongs to the dimethyl sulfoxide (DMSO) reductase family, but has a different substrate specificity than its homologous enzyme. While the DMSO reductases reduce a broad spectra of organic S-oxide and N-oxide compounds, TMAO reductase from Shewanella massilia reduces only TMAO as the natural compound. The crystal structure was solved by molecular replacement with the coordinates of the DMSO reductase from Rhodobacter sphaeroides. The overall fold of the protein structure is essentially the same as the DMSO reductase structures, organized into four domains. The molybdenum coordination sphere is closest to that described in the DMSO reductase of Rhodobacter capsulatus. The structural differences found in the protein environment of the active site could be related to the differences in substrate specificity of these enzymes. In close vicinity of the molybdenum ion a tyrosine residue is missing in the TMAO reductase, leaving a greater space accessible to the solvent. This tyrosine residue has contacts to the oxo groups in the DMSO reductase structures. The arrangement and number of charged residues lining the inner surface of the funnel-like entrance to the active site, is different in the TMAO reductase than in the DMSO reductases from Rhodobacter species. Furthermore a surface loop at the top of the active-site funnel, for which no density was present in the DMSO reductase structures, is well defined in the oxidized form of the TMAO reductase structure, and is located on the border of the funnel-like entrance of the active center.


===TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA===
Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution.,Czjzek M, Dos Santos JP, Pommier J, Giordano G, Mejean V, Haser R J Mol Biol. 1998 Nov 27;284(2):435-47. PMID:9813128<ref>PMID:9813128</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 9813128 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_9813128}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1TMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_massilia Shewanella massilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMO OCA].
 
==Reference==
Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution., Czjzek M, Dos Santos JP, Pommier J, Giordano G, Mejean V, Haser R, J Mol Biol. 1998 Nov 27;284(2):435-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9813128 9813128]
[[Category: Shewanella massilia]]
[[Category: Shewanella massilia]]
[[Category: Single protein]]
[[Category: Czjzek M]]
[[Category: Trimethylamine-N-oxide reductase]]
[[Category: Dos Santos JP]]
[[Category: Czjzek, M.]]
[[Category: Giordano G]]
[[Category: Giordano, G.]]
[[Category: Mejean V]]
[[Category: Mejean, V.]]
[[Category: Santos, J P.Dos.]]
[[Category: Mo-cofactor]]
[[Category: Molybdenum]]
[[Category: Molybdoenzyme]]
[[Category: Oxidoreductase]]
[[Category: Oxotransferase]]
[[Category: Tmao reductase]]
 
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