CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.40 | 3-Layer(aba) Sandwich | 
|   | 3.40.30 | Glutaredoxin | 
|   | 3.40.30.10 | Glutaredoxin | 
Domain Context
CATH Clusters
| Superfamily | Glutaredoxin | 
| Functional Family | Peptide methionine sulfoxide reductase | 
Enzyme Information
| 1.8.4.11 | Peptide-methionine (S)-S-oxide reductase. based on mapping to UniProt Q9JWM8 (1) Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (S)-S-oxide + thioredoxin. (2) L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S- oxide + thioredoxin. -!- The reaction occurs in the reverse direction to that shown above. -!- Exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid. -!- On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly. -!- 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. -!- Formerly EC 1.8.4.6. | 
| 1.8.4.12 | Peptide-methionine (R)-S-oxide reductase. based on mapping to UniProt Q9JWM8 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)
| Q9JWM8 | MSRAB_NEIMA Neisseria meningitidis Z2491 Peptide methionine sulfoxide reductase MsrA/MsrB | 
PDB Structure
| PDB | 2FY6 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | The X-ray Structure of the N-terminal Domain of PILB from Neisseria meningitidis Reveals a Thioredoxin-fold J.Mol.Biol. | 
