› 1p09

X-ray diffraction
2.2Å resolution

STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES

Released:
DOI: 10.2210/pdb1p09/pdb
PDB entry 1p09 coloured by chain, front view.
PDB entry 1p09 coloured by chain, side view.
PDB entry 1p09 coloured by chain, top view.
Source organism: Lysobacter enzymogenes
Primary publication:
Structural plasticity broadens the specificity of an engineered protease.
Bone R, Silen JL, Agard DA
Nature 339 191-5 (1989)
PMID: 2716847

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Ala-|-, Val-|- in bacterial cell walls, elastin and other proteins.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-lytic protease Chain: A
Molecule details ›
Chain: A
Length: 198 amino acids
Theoretical weight: 19.82 KDa
Source organism: Lysobacter enzymogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P00778 (Residues: 200-397; Coverage: 53%)
Gene name: alpha-LP
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 66.28Å b: 66.28Å c: 80.18Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.135 not available not available
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Enzyme promiscuity: a mechanistic and evolutionary perspective.
Khersonsky et al. (2010)
14 more