› 1x60

Solution NMR

Solution structure of the peptidoglycan binding domain of B. subtilis cell wall lytic enzyme CwlC

Released:
DOI: 10.2210/pdb1x60/pdb
PDB entry 1x60 coloured by chain, ensemble of 30 models, front view.
PDB entry 1x60 coloured by chain, ensemble of 30 models, side view.
PDB entry 1x60 coloured by chain, ensemble of 30 models, top view.
Source organism: Bacillus subtilis
Primary publication:
Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Mishima M, Shida T, Yabuki K, Kato K, Sekiguchi J, Kojima C
Biochemistry 44 10153-63 (2005)
PMID: 16042392

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170329 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sporulation-specific N-acetylmuramoyl-L-alanine amidase Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.26 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q06320 (Residues: 177-255; Coverage: 31%)
Gene names: BSU17410, cwlC
Sequence domains: SPOR domain
Structure domains: Sporulation related repeat

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Regulation of bacterial cell wall growth.
Egan et al. (2017)
4 more

11 mentions without citation

Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification.
Wolff et al. (2007)
10 more