1tmo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:40, 14 February 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1tmo.jpg|left|200px]]<br /><applet load="1tmo" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1tmo, resolution 2.5&Aring;" />
 
-
'''TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA'''<br />
 
-
==Overview==
+
==TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA==
-
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.
+
<StructureSection load='1tmo' size='340' side='right'caption='[[1tmo]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<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>
-
1TMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_massilia Shewanella massilia] with 2MD and 2MO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trimethylamine-N-oxide_reductase Trimethylamine-N-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.6.9 1.6.6.9] Known structural/functional Site: <scene name='pdbsite=MOS:Mo Cofactor Binding The Mo Ion, Also Ligated By Two Oxo ...'>MOS</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TMO 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]] 2.5&#8491;</td></tr>
-
 
+
<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>
-
==Reference==
+
<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>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9813128 9813128]
+
</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/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=1tmo ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[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: 2MD]]
+
-
[[Category: 2MO]]
+
-
[[Category: bis (molybdopterin guanine dinucleotide)]]
+
-
[[Category: mo-cofactor]]
+
-
[[Category: molybdenum]]
+
-
[[Category: molybdoenzyme]]
+
-
[[Category: oxidoreductase]]
+
-
[[Category: oxotransferase]]
+
-
[[Category: tmao reductase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:02:18 2007''
+

Current revision

TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA

PDB ID 1tmo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tmo"
Personal tools