User:Eduarda Franco Marcolino/Sandbox 1

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Function

Reactive oxygen species (ROS) and nitrogen intermediates can cause cellular damage. Cells have developed several mechanisms to eliminate these reactive molecules or repair the damage. Among proteins, one of the amino acids most easily oxidized is methionine, which is converted into methionine sulfoxide. The enzyme peptide methionine sulfoxide reductase (MsrA) catalyzes the reduction of methionine sulfoxide back to methionine, both in proteins and as free methionine. MsrA plays an important role in protecting the cell against oxidative damage.

Disease

Relevance

Structural highlights

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. MsrAs contain within their presumed active sites a conserved Gly-Cys-Phe-Trp-Gly motif

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