CATH Classification

Domain Context

CATH Clusters

Superfamily Peptide methionine sulfoxide reductase.
Functional Family Peptide methionine sulfoxide reductase MsrB

Enzyme Information

1.8.4.12
Peptide-methionine (R)-S-oxide reductase.
based on mapping to UniProt P54155
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (R)-S-oxide + thioredoxin.
-!- The reaction occurs in the reverse direction to that shown above. -!- Exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide. -!- While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater. -!- Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. -!- The reaction proceeds via a sulfenic-acid intermediate. -!- For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well.

UniProtKB Entries (1)

P54155
MSRB_BACSU
Bacillus subtilis subsp. subtilis str. 168
Peptide methionine sulfoxide reductase MsrB

PDB Structure

PDB 2KZN
External Links
Method SOLUTION NMR
Organism
Primary Citation
Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples.
Lange, O.F., Rossi, P., Sgourakis, N.G., Song, Y., Lee, H.W., Aramini, J.M., Ertekin, A., Xiao, R., Acton, T.B., Montelione, G.T., Baker, D.
Proc.Natl.Acad.Sci.USA