› 2v2e

X-ray diffraction
1.68Å resolution

Structure of isoniazid (INH) bound to cytochrome c peroxidase mutant N184R Y36A

Released:
DOI: 10.2210/pdb2v2e/pdb
PDB entry 2v2e coloured by chain, front view.
PDB entry 2v2e coloured by chain, side view.
PDB entry 2v2e coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The tuberculosis prodrug isoniazid bound to activating peroxidases.
Metcalfe C, Macdonald IK, Murphy EJ, Brown KA, Raven EL, Moody PC
J Biol Chem 283 6193-200 (2008)
PMID: 18056997

Function and Biology Details

Reaction catalysed: 
2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132475 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c peroxidase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.58 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00431 (Residues: 71-361; Coverage: 81%)
Gene names: CCP, CCP1, CPO, YKR066C
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand ISZ 1 x ISZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 51.147Å b: 75.13Å c: 106.864Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.187
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Overview on mechanisms of isoniazid action and resistance in Mycobacterium tuberculosis.
Unissa et al. (2016)
4 more

1 mention without citation

Antibiotic resistance in Mycobacterium tuberculosis: peroxidase intermediate bypass causes poor isoniazid activation by the S315G mutant of M. tuberculosis catalase-peroxidase (KatG).
Suarez et al. (2009)