7e43

X-ray diffraction
2.2Å resolution

Structural insights into a bifunctional peptide methionine sulfoxide reductase MsrA/B fusion protein from Helicobacter pylori

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-127701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide methionine sulfoxide reductase MsrA/MsrB Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 41.31 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: O25011 (Residues: 1-359; Coverage: 100%)
Gene names: HP_0224, msrA, msrAB
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 11C
Spacegroup: P1
Unit cell:
a: 52.125Å b: 72.505Å c: 82.23Å
α: 93.16° β: 93.8° γ: 111.08°
R-values:
R R work R free
0.189 0.188 0.214
Expression system: Escherichia coli K-12