› 3t38

X-ray diffraction
2.2Å resolution

Corynebacterium glutamicum thioredoxin-dependent arsenate reductase Cg_ArsC1'

Released:
DOI: 10.2210/pdb3t38/pdb
PDB entry 3t38 coloured by chain, front view.
PDB entry 3t38 coloured by chain, side view.
PDB entry 3t38 coloured by chain, top view.
Source organism: Corynebacterium glutamicum
Primary publication:
Corynebacterium glutamicum survives arsenic stress with arsenate reductases coupled to two distinct redox mechanisms.
Villadangos AF, Van Belle K, Wahni K, Dufe VT, Freitas S, Nur H, De Galan S, Gil JA, Collet JF, Mateos LM, Messens J
Mol Microbiol 82 998-1014 (2011)
PMID: 22032722

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphotyrosine protein phosphatase I domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 213 amino acids
Theoretical weight: 23.5 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8NQC6 (Residues: 1-213; Coverage: 100%)
Gene name: Cgl1512
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand D1D 1 x D1D
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 41.8Å b: 75.5Å c: 58.1Å
α: 90° β: 100.5° γ: 90°
R-values:
R R work R free
0.18 0.177 0.231
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Understanding the pK(a) of redox cysteines: the key role of hydrogen bonding.
Roos et al. (2013)
4 more

1 mention without citation

Enzyme structure captures four cysteines aligned for disulfide relay.
Gat et al. (2014)