› 2wwc

X-ray diffraction
1.75Å resolution

3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand

Released:
DOI: 10.2210/pdb2wwc/pdb
PDB entry 2wwc coloured by chain, front view.
PDB entry 2wwc coloured by chain, side view.
PDB entry 2wwc coloured by chain, top view.
Source organism: Streptococcus pneumoniae R6
Primary publication:
Insights into pneumococcal fratricide from the crystal structures of the modular killing factor LytC.
Pérez-Dorado I, González A, Morales M, Sanles R, Striker W, Vollmer W, Mobashery S, García JL, Martínez-Ripoll M, García P, Hermoso JA
Nat Struct Mol Biol 17 576-81 (2010)
PMID: 20400948

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,4-beta-N-acetylmuramidase Chain: A
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 55.27 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8DP07 (Residues: 34-501; Coverage: 100%)
Gene names: lytC, spr1431
Sequence domains:
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand GOL 14 x GOL
Ligand CHT 8 x CHT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 59.54Å b: 68.8Å c: 75.64Å
α: 90° β: 105.45° γ: 90°
R-values:
R R work R free
0.176 0.174 0.203
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Lipoteichoic acid synthesis and function in gram-positive bacteria.
Percy et al. (2014)
8 more

3 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)
2 more