› 1yb0

X-ray diffraction
1.86Å resolution

Structure of PlyL

Released:
DOI: 10.2210/pdb1yb0/pdb
PDB entry 1yb0 coloured by chain, front view.
PDB entry 1yb0 coloured by chain, side view.
PDB entry 1yb0 coloured by chain, top view.
Source organism: Bacillus anthracis
Primary publication:
Structure and lytic activity of a Bacillus anthracis prophage endolysin.
Low LY, Yang C, Perego M, Osterman A, Liddington RC
J Biol Chem 280 35433-9 (2005)
PMID: 16103125

Function and Biology Details

Reaction catalysed: 
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105639 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylmuramoyl-L-alanine amidase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 159 amino acids
Theoretical weight: 18.09 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A6H3AMF3 (Residues: 1-159; Coverage: 68%)
Gene name: GBAA_4073
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like

Ligands and Environments

2 bound ligands:
Ligand ZN 3 x ZN
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R, SSRL BEAMLINE BL11-1
Spacegroup: P61
Unit cell:
a: 163.181Å b: 163.181Å c: 37.292Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

Bacterial peptidoglycan (murein) hydrolases.
Vollmer et al. (2008)
24 more

6 mentions without citation

Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin.
Gu et al. (2014)
5 more