› 2e00

X-ray diffraction
2Å resolution

Crystal structure of N392L mutant of yeast bleomycin hydrolase

Released:
DOI: 10.2210/pdb2e00/pdb
Model geometry
Fit model/data
PDB entry 2e00 coloured by chain, front view.
PDB entry 2e00 coloured by chain, side view.
PDB entry 2e00 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure.
O'Farrell PA, Joshua-Tor L
Biochem J 401 421-8 (2007)
PMID: 17007609

Function and Biology Details

Reaction catalysed: 
Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred (1).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine proteinase 1, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 457 amino acids
Theoretical weight: 52.43 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01532 (Residues: 30-482; Coverage: 94%)
  • Best match: Q01532-2 (Residues: 1-453)
Gene names: BLH1, GAL6, LAP3, N1118, YCP1, YNL239W
Sequence domains: Peptidase C1-like family
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P6322
Unit cell:
a: 150.878Å b: 150.878Å c: 89.84Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.212 0.248
Expression system: Escherichia coli

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Citations

7 citation in other articles

Single-nucleotide polymorphic variants of human glutathione transferase T1-1 differ in stability and functional properties.
Josephy et al. (2009)
6 more

1 mention without citation

Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure.
O'Farrell et al. (2007)