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[[Image:1fvg.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF BOVINE PEPTIDE METHIONINE SULFOXIDE REDUCTASE==
|PDB= 1fvg |SIZE=350|CAPTION= <scene name='initialview01'>1fvg</scene>, resolution 1.6&Aring;
<StructureSection load='1fvg' size='340' side='right'caption='[[1fvg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
<table><tr><td colspan='2'>[[1fvg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FVG FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-methionine-(S)-S-oxide_reductase Peptide-methionine-(S)-S-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.11 1.8.4.11] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvg OCA], [https://pdbe.org/1fvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fvg RCSB], [https://www.ebi.ac.uk/pdbsum/1fvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fvg ProSAT]</span></td></tr>
|RELATEDENTRY=[[1fva|1FVA]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvg OCA], [http://www.ebi.ac.uk/pdbsum/1fvg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fvg RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/MSRA_BOVIN MSRA_BOVIN] Has 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.
 
== Evolutionary Conservation ==
'''CRYSTAL STRUCTURE OF BOVINE PEPTIDE METHIONINE SULFOXIDE REDUCTASE'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/1fvg_consurf.spt"</scriptWhenChecked>
Peptide methionine sulfoxide reductase (MsrA) reverses oxidative damage to both free methionine and methionine within proteins. As such, it helps protect the host organism against stochastic damage that can contribute to cell death. The structure of bovine MsrA has been determined in two different modifications, both of which provide different insights into the biology of the protein. There are three cysteine residues located in the vicinity of the active site. Conformational changes in a glycine-rich C-terminal tail appear to allow all three thiols to come together and to participate in catalysis. The structures support a unique, thiol-disulfide exchange mechanism that relies upon an essential cysteine as a nucleophile and additional conserved residues that interact with the oxygen atom of the sulfoxide moiety.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1FVG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVG OCA].  
</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=1fvg ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme., Lowther WT, Brot N, Weissbach H, Matthews BW, Biochemistry. 2000 Nov 7;39(44):13307-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11063566 11063566]
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Peptide-methionine-(S)-S-oxide reductase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Brot N]]
[[Category: Brot, N.]]
[[Category: Lowther WT]]
[[Category: Lowther, W T.]]
[[Category: Matthews BW]]
[[Category: Matthews, B W.]]
[[Category: Weissbach H]]
[[Category: Weissbach, H.]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:31:01 2008''

Latest revision as of 14:16, 27 March 2024

CRYSTAL STRUCTURE OF BOVINE PEPTIDE METHIONINE SULFOXIDE REDUCTASECRYSTAL STRUCTURE OF BOVINE PEPTIDE METHIONINE SULFOXIDE REDUCTASE

Structural highlights

1fvg is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MSRA_BOVIN Has 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.

Evolutionary Conservation

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

1fvg, resolution 1.60Å

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