› 4m09

X-ray diffraction
2.45Å resolution

Crystal Structure of Mutant Chlorite Dismutase from Candidatus Nitrospira defluvii W146Y R173Q

Released:
DOI: 10.2210/pdb4m09/pdb
PDB entry 4m09 coloured by chain, front view.
PDB entry 4m09 coloured by chain, side view.
PDB entry 4m09 coloured by chain, top view.
Source organism: Nitrospira defluvii
Primary publication:
Manipulating conserved heme cavity residues of chlorite dismutase: effect on structure, redox chemistry, and reactivity.
Hofbauer S, Gysel K, Bellei M, Hagmüller A, Schaffner I, Mlynek G, Kostan J, Pirker KF, Daims H, Furtmüller PG, Battistuzzi G, Djinović-Carugo K, Obinger C
Biochemistry 53 77-89 (2014)
PMID: 24364531

Function and Biology Details

Reaction catalysed: 
Chloride + O(2) = chlorite
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109924 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chlorite dismutase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 241 amino acids
Theoretical weight: 27.43 KDa
Source organism: Nitrospira defluvii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B3U4H7 (Residues: 27-264; Coverage: 100%)
Gene names: NIDE1387, cld, cld1
Sequence domains: Chlorite dismutase

Ligands and Environments


Cofactor: Ligand HEM 5 x HEM
3 bound ligands:
Ligand SO4 9 x SO4
Ligand EDO 9 x EDO
Ligand IMD 2 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 138.1Å b: 114.98Å c: 118.87Å
α: 90° β: 118.08° γ: 90°
R-values:
R R work R free
0.28 0.277 0.332
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme synthesis in Firmicutes and Actinobacteria.
Dailey et al. (2015)
2 more

3 mentions without citation

Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme.
Celis et al. (2015)
2 more