› 1oba

X-ray diffraction
2.45Å resolution

Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1 complexed with choline

Released:
DOI: 10.2210/pdb1oba/pdb
PDB entry 1oba coloured by chain, front view.
PDB entry 1oba coloured by chain, side view.
PDB entry 1oba coloured by chain, top view.
Source organism: Streptococcus phage Cp1
Primary publication:
Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.
Hermoso JA, Monterroso B, Albert A, Galán B, Ahrazem O, García P, Martínez-Ripoll M, García JL, Menéndez M
Structure 11 1239-49 (2003)
PMID: 14527392

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147205 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 39.28 KDa
Source organism: Streptococcus phage Cp1
Expression system: Escherichia coli
UniProt:
  • Canonical: P15057 (Residues: 1-339; Coverage: 100%)
Gene names: 22, CPL1
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 78.03Å b: 95.95Å c: 129.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.264
Expression system: Escherichia coli

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Citations

21 review citations

Bacteriophage endolysins as novel antimicrobials.
Schmelcher et al. (2012)
20 more

4 mentions without citation

Choline Binding Proteins from Streptococcus pneumoniae: A Dual Role as Enzybiotics and Targets for the Design of New Antimicrobials.
Maestro et al. (2016)
3 more