PDBe 4ger

X-ray diffraction
1.59Å resolution

Crystal structure of Gentlyase, the neutral metalloprotease of Paenibacillus polymyxa

Released:
Source organism: Paenibacillus polymyxa
Primary publication:
Structure of Gentlyase, the neutral metalloprotease of Paenibacillus polymyxa.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 69 24-31 (2013)
PMID: 23275160

Function and Biology Details

Reaction catalysed:
Similar, but not identical, to that of thermolysin. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacillolysin Chains: A, B
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 32.41 KDa
Source organism: Paenibacillus polymyxa
Expression system: Bacillus amyloliquefaciens
UniProt:
  • Canonical: P29148 (Residues: 289-590; Coverage: 53%)
Gene name: npr
Sequence domains: Thermolysin metallopeptidase, alpha-helical domain
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 61.014Å b: 77.07Å c: 64.052Å
α: 90° β: 103.16° γ: 90°
R-values:
R R work R free
0.202 0.2 0.243
Expression system: Bacillus amyloliquefaciens