› 3pil

X-ray diffraction
2.04Å resolution

Crystal structure of Mxr1 from Saccharomyces cerevisiae in reduced form

Released:
DOI: 10.2210/pdb3pil/pdb
PDB entry 3pil coloured by chain, front view.
PDB entry 3pil coloured by chain, side view.
PDB entry 3pil coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1.
Ma XX, Guo PC, Shi WW, Luo M, Tan XF, Chen Y, Zhou CZ
J Biol Chem 286 13430-7 (2011)
PMID: 21345799

Function and Biology Details

Reaction catalysed: 
L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154004 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide methionine sulfoxide reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 184 amino acids
Theoretical weight: 21.1 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P40029 (Residues: 2-184; Coverage: 100%)
Gene names: MXR1, YER042W
Sequence domains: Peptide methionine sulfoxide reductase
Structure domains: Peptide methionine sulphoxide reductase MsrA

Ligands and Environments

1 bound ligand:
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 64.31Å b: 70.14Å c: 74.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.247
Expression system: Escherichia coli

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Citations

5 review citations

The physiological role of reversible methionine oxidation.
Drazic et al. (2014)
4 more

4 mentions without citation

The bacterial outer membrane β-barrel assembly machinery.
Kim et al. (2012)
3 more