› 2pro

X-ray diffraction
3Å resolution

PRO REGION OF ALPHA-LYTIC PROTEASE

Released:
DOI: 10.2210/pdb2pro/pdb
PDB entry 2pro coloured by chain, front view.
PDB entry 2pro coloured by chain, side view.
PDB entry 2pro coloured by chain, top view.
Source organism: Lysobacter enzymogenes
Primary publication:
Structure of alpha-lytic protease complexed with its pro region.
Sauter NK, Mau T, Rader SD, Agard DA
Nat Struct Biol 5 945-50 (1998)
PMID: 9808037

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Ala-|-, Val-|- in bacterial cell walls, elastin and other proteins.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-133493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-lytic protease Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 166 amino acids
Theoretical weight: 17.84 KDa
Source organism: Lysobacter enzymogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P00778 (Residues: 34-199; Coverage: 45%)
Gene name: alpha-LP
Sequence domains: Alpha-lytic protease prodomain
Structure domains: GMP Synthetase; Chain A, domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P1
Unit cell:
a: 47.6Å b: 54.7Å c: 64Å
α: 104° β: 102.5° γ: 91.9°
R-values:
R R work R free
0.202 0.202 0.342
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The intramolecular chaperone-mediated protein folding.
Chen et al. (2008)
6 more

8 mentions without citation

Allosteric regulation of CRISPR-Cas9 for DNA-targeting and cleavage.
Zuo et al. (2020)
7 more