Structure and Mechanism of Peptide Methionine Sulfoxide Reductase, an “Anti-Oxidation” Enzyme ,
2000; American Chemical Society; Volume: 39; Issue: 44 Linguagem: Inglês
10.1021/bi0020269
ISSN1943-295X
AutoresW. Todd Lowther, Nathan Brot, Herbert Weissbach, Brian W. Matthews,
Tópico(s)Electron Spin Resonance Studies
ResumoPeptide 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.
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