1fva

From Proteopedia

(Difference between revisions)

Current revision

CRYSTAL STRUCTURE OF BOVINE METHIONINE SULFOXIDE REDUCTASE

Structural highlights

1fva is a 2 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 1.7Å
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.

Publication Abstract from PubMed

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.

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:11063566^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lowther WT, Brot N, Weissbach H, Matthews BW. Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme. Biochemistry. 2000 Nov 7;39(44):13307-12. PMID:11063566

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fva"

@@ Line 3: / Line 3: @@
 <StructureSection load='1fva' size='340' side='right'caption='[[1fva]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fva]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FVA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fva]] is a 2 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=1FVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FVA FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fvg|1fvg]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptide-methionine_(S)-S-oxide_reductase Peptide-methionine (S)-S-oxide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.11 1.8.4.11] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fva OCA], [https://pdbe.org/1fva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fva RCSB], [https://www.ebi.ac.uk/pdbsum/1fva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fva ProSAT]</span></td></tr>
 </table>
 == 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.
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 32: @@
 __TOC__
 </StructureSection>
+[[Category: Bos taurus]]
 [[Category: Large Structures]]
-[[Category: Brot, N]]
+[[Category: Brot N]]
-[[Category: Lowther, W T]]
+[[Category: Lowther WT]]
-[[Category: Matthews, B W]]
+[[Category: Matthews BW]]
-[[Category: Weissbach, H]]
+[[Category: Weissbach H]]
-[[Category: Oxidoreductase]]

1fva

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF BOVINE METHIONINE SULFOXIDE REDUCTASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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