› 2bml

X-ray diffraction
2.6Å resolution

Ofloxacin-like antibiotics inhibit pneumococcal cell wall degrading virulence factors

Released:
DOI: 10.2210/pdb2bml/pdb
PDB entry 2bml coloured by chain, front view.
PDB entry 2bml coloured by chain, side view.
PDB entry 2bml coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Ofloxacin-like antibiotics inhibit pneumococcal cell wall-degrading virulence factors.
Fernández-Tornero C, García E, de Pascual-Teresa B, López R, Giménez-Gallego G, Romero A
J Biol Chem 280 19948-57 (2005)
PMID: 15769740

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139117 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Autolysin Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 14.89 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P06653 (Residues: 193-318; Coverage: 40%)
Gene names: SP_1937, lytA
Sequence domains:
Structure domains: Cholin Binding

Ligands and Environments

5 bound ligands:
Ligand TRS 2 x TRS
Ligand P6G 2 x P6G
Ligand XED 1 x XED
Ligand PG4 1 x PG4
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21212
Unit cell:
a: 101.67Å b: 94.48Å c: 38.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.28
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Crystal structure of receptor-binding C-terminal repeats from Clostridium difficile toxin A.
Ho et al. (2005)
7 more

5 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)
4 more