› 1hcx

X-ray diffraction
2.6Å resolution

Choline binding domain of the major autolysin (C-LytA) from Streptococcus pneumoniae

Released:
DOI: 10.2210/pdb1hcx/pdb
PDB entry 1hcx coloured by chain, front view.
PDB entry 1hcx coloured by chain, side view.
PDB entry 1hcx coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA.
Fernández-Tornero C, López R, García E, Giménez-Gallego G, Romero A
Nat Struct Biol 8 1020-4 (2001)
PMID: 11694890

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: 127 amino acids
Theoretical weight: 14.95 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P06653 (Residues: 192-318; Coverage: 40%)
Gene names: SP_1937, lytA
Sequence domains:
Structure domains: Cholin Binding

Ligands and Environments

3 bound ligands:
Ligand TPT 1 x TPT
Ligand CHT 5 x CHT
Ligand DDQ 2 x DDQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: I222
Unit cell:
a: 58.049Å b: 118.177Å c: 104.859Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.239 0.302
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Bacterial peptidoglycan (murein) hydrolases.
Vollmer et al. (2008)
13 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