› 3a9l

X-ray diffraction
1.9Å resolution

Structure of Bacteriophage poly-gamma-glutamate hydrolase

Released:
DOI: 10.2210/pdb3a9l/pdb
PDB entry 3a9l coloured by chain, front view.
PDB entry 3a9l coloured by chain, side view.
PDB entry 3a9l coloured by chain, top view.
Source organism: Bacillus phage phiNIT1
Primary publication:
Crystal structure of bacteriophage ϕNIT1 zinc peptidase PghP that hydrolyzes γ-glutamyl linkage of bacterial poly-γ-glutamate.
Fujimoto Z, Kimura K
Proteins 80 722-32 (2012)
PMID: 22105902

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183086 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly-gamma-glutamate hydrolase of phage (PghP) Chains: A, B
Molecule details ›
Chains: A, B
Length: 216 amino acids
Theoretical weight: 24.03 KDa
Source organism: Bacillus phage phiNIT1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q852V1 (Residues: 1-208; Coverage: 100%)
Gene name: pghP
Sequence domains: Poly-gamma-glutamate hydrolase
Structure domains: Poly-gamma-glutamate hydrolase, zinc-binding motif

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P32
Unit cell:
a: 86.809Å b: 86.809Å c: 85.116Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.283 0.281 0.315
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Effects of actin-like proteins encoded by two Bacillus pumilus phages on unstable lysogeny, revealed by genomic analysis.
Yuan et al. (2015)
2 more

3 mentions without citation

γ-PGA Hydrolases of Phage Origin in Bacillus subtilis and Other Microbial Genomes.
Mamberti et al. (2015)
2 more