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1ff3

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(New page: 200px<br /><applet load="1ff3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ff3, resolution 1.9&Aring;" /> '''STRUCTURE OF THE PEPT...)
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[[Image:1ff3.jpg|left|200px]]<br /><applet load="1ff3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ff3, resolution 1.9&Aring;" />
 
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'''STRUCTURE OF THE PEPTIDE METHIONINE SULFOXIDE REDUCTASE FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==STRUCTURE OF THE PEPTIDE METHIONINE SULFOXIDE REDUCTASE FROM ESCHERICHIA COLI==
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BACKGROUND: Peptide methionine sulphoxide reductases catalyze the, reduction of oxidized methionine residues in proteins. They are implicated, in the defense of organisms against oxidative stress and in the regulation, of processes involving peptide methionine oxidation/reduction. These, enzymes are found in numerous organisms, from bacteria to mammals and, plants. Their primary structure shows no significant similarity to any, other known protein. RESULTS: The X-ray structure of the peptide, methionine sulphoxide reductase from Escherichia coli was determined at 3, A resolution by the multiple wavelength anomalous dispersion method for, the selenomethionine-substituted enzyme, and it was refined to 1.9 A, resolution for the native enzyme. The 23 kDa protein is folded into an, alpha/beta roll and contains a large proportion of coils. Among the three, cysteine residues involved in the catalytic mechanism, Cys-51 is, positioned at the N terminus of an alpha helix, in a solvent-exposed area, composed of highly conserved amino acids. The two others, Cys-198 and, Cys-206, are located in the C-terminal coil. CONCLUSIONS: Sequence, alignments show that the overall fold of the peptide methionine sulphoxide, reductase from E. coli is likely to be conserved in many species. The, characteristics observed in the Cys-51 environment are in agreement with, the expected accessibility of the active site of an enzyme that reduces, methionine sulphoxides in various proteins. Cys-51 could be activated by, the influence of an alpha helix dipole. The involvement of the two other, cysteine residues in the catalytic mechanism requires a movement of the, C-terminal coil. Several conserved amino acids and water molecules are, discussed as potential participants in the reaction.
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<StructureSection load='1ff3' size='340' side='right'caption='[[1ff3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ff3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FF3 FirstGlance]. <br>
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1FF3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FF3 OCA].
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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]] 1.9&#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=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1ff3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ff3 OCA], [https://pdbe.org/1ff3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ff3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ff3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ff3 ProSAT]</span></td></tr>
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Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution., Tete-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G, Aubry A, Structure. 2000 Nov 15;8(11):1167-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11080639 11080639]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MSRA_ECOLI MSRA_ECOLI] Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.[HAMAP-Rule:MF_01401]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/1ff3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=1ff3 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aubry, A.]]
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[[Category: Aubry A]]
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[[Category: Azza, S.]]
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[[Category: Azza S]]
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[[Category: Boschi-Muller, S.]]
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[[Category: Boschi-Muller S]]
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[[Category: Branlant, G.]]
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[[Category: Branlant G]]
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[[Category: Cobessi, D.]]
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[[Category: Cobessi D]]
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[[Category: Tete-Favier, F.]]
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[[Category: Tete-Favier F]]
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[[Category: SO4]]
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[[Category: alpha beta roll]]
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[[Category: msra]]
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[[Category: peptide methionine sulfoxide reductase]]
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[[Category: pmsr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:52:06 2007''
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Current revision

STRUCTURE OF THE PEPTIDE METHIONINE SULFOXIDE REDUCTASE FROM ESCHERICHIA COLI

PDB ID 1ff3

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