› 1h7k

X-ray diffraction
2.4Å resolution

Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity

Released:
DOI: 10.2210/pdb1h7k/pdb
PDB entry 1h7k coloured by chain, front view.
PDB entry 1h7k coloured by chain, side view.
PDB entry 1h7k coloured by chain, top view.
Source organism: Proteus mirabilis
Primary publication:
Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity.
Andreoletti P, Gambarelli S, Sainz G, Stojanoff V, White C, Desfonds G, Gagnon J, Gaillard J, Jouve HM
Biochemistry 40 13734-43 (2001)
PMID: 11695923

Function and Biology Details

Reaction catalysed: 
2 H(2)O(2) = O(2) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154608 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase Chain: A
Molecule details ›
Chain: A
Length: 483 amino acids
Theoretical weight: 55.61 KDa
Source organism: Proteus mirabilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P42321 (Residues: 2-484; Coverage: 100%)
Gene name: katA
Sequence domains:
Structure domains: Catalase core domain

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
2 bound ligands:
Ligand ACT 1 x ACT
Ligand SO4 1 x SO4
1 modified residue:
Ligand OMT 1 x OMT

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P6222
Unit cell:
a: 110Å b: 110Å c: 251.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.237 0.237 0.24
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Mammalian catalase: a venerable enzyme with new mysteries.
Kirkman et al. (2007)
3 more

1 mention without citation

Monofunctional Heme-Catalases.
Hansberg W. (2022)