› 4m06

X-ray diffraction
2.6Å resolution

Crystal Structure of Mutant Chlorite Dismutase from Candidatus Nitrospira defluvii W145F in Complex with Cyanide

Released:
DOI: 10.2210/pdb4m06/pdb
PDB entry 4m06 coloured by chain, front view.
PDB entry 4m06 coloured by chain, side view.
PDB entry 4m06 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
OpenAccess logo 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: 260 amino acids
Theoretical weight: 29.75 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 GOL 1 x GOL
Ligand CYN 5 x CYN
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 136.21Å b: 113.42Å c: 118.84Å
α: 90° β: 117.94° γ: 90°
R-values:
R R work R free
0.213 0.211 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

2 mentions without citation

Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.
Hofbauer et al. (2016)
1 more