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 Q3JRF0
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)

Q3JRF0
MSRB_BURP1
Burkholderia pseudomallei 1710b
Peptide methionine sulfoxide reductase MsrB

PDB Structure

PDB 3CXK
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The plug-based nanovolume Microcapillary Protein Crystallization System (MPCS).
Gerdts, C.J., Elliott, M., Lovell, S., Mixon, M.B., Napuli, A.J., Staker, B.L., Nollert, P., Stewart, L.
Acta Crystallogr.,Sect.D
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