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Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme.

Lowther WT, Brot N, Weissbach H, Matthews BW
Biochemistry 39 13307-12 (2000)
Cited: 78 times
EuropePMC logo PMID: 11063566

Abstract

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.

Reviews - 1fva mentioned but not cited (1)

  1. The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions. Kim HY. Antioxid Redox Signal 19 958-969 (2013)

Articles - 1fva mentioned but not cited (4)

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Related citations provided by authors (1)

  1. Thiol-disulfide Exchange is Involved in the Catalytic Mechanism of Peptide Methionine Sulfoxide Reductase. Lowther WT, Brot N, Weissbach H, Honek JF, Matthews BW Proc. Natl. Acad. Sci. U.S.A. 97 6463-6468 (2000)

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