› 3e0o

X-ray diffraction
2.6Å resolution

Crystal structure of MsrB

Released:
DOI: 10.2210/pdb3e0o/pdb
PDB entry 3e0o coloured by chain, front view.
PDB entry 3e0o coloured by chain, side view.
PDB entry 3e0o coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae.
Kim YK, Shin YJ, Lee WH, Kim HY, Hwang KY
Mol Microbiol 72 699-709 (2009)
PMID: 19400786

Function and Biology Details

Reaction catalysed: 
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo hexamer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156951 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide methionine sulfoxide reductase MsrB Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 144 amino acids
Theoretical weight: 16.76 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P54155 (Residues: 1-143; Coverage: 100%)
Gene names: BSU21680, msrB, yppQ
Sequence domains: SelR domain
Structure domains: Peptide methionine sulfoxide reductase.

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P3
Unit cell:
a: 136.114Å b: 136.114Å c: 61.925Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.235 0.294
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Selenoproteins: molecular pathways and physiological roles.
Labunskyy et al. (2014)
5 more

7 mentions without citation

A community resource of experimental data for NMR / X-ray crystal structure pairs.
Everett et al. (2016)
6 more