› 4ct3

X-ray diffraction
1.69Å resolution

Methylmercury chloride derivative structure of the lytic CHAPK domain of the endolysin LysK from Staphylococcus aureus bacteriophage K

Released:
DOI: 10.2210/pdb4ct3/pdb
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PDB entry 4ct3 coloured by chain, side view.
PDB entry 4ct3 coloured by chain, top view.
Source organism: Staphylococcus virus K
Primary publication:
Crystal structure of the lytic CHAP(K) domain of the endolysin LysK from Staphylococcus aureus bacteriophage K.
Sanz-Gaitero M, Keary R, Garcia-Doval C, Coffey A, van Raaij MJ
OpenAccess logo Virol J 11 133 (2014)
PMID: 25064136

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180546 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin LysK Chains: E, G, I, K
Molecule details ›
Chains: E, G, I, K
Length: 165 amino acids
Theoretical weight: 18.83 KDa
Source organism: Staphylococcus virus K
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6Y7T6 (Residues: 1-165; Coverage: 33%)
Gene names: ORF30/ORF32, PhageK_071
Sequence domains: CHAP domain

Ligands and Environments

6 bound ligands:
Ligand CL 2 x CL
Ligand GOL 2 x GOL
Ligand EPE 4 x EPE
Ligand CA 4 x CA
Ligand MMC 8 x MMC
Ligand HG 6 x HG
1 modified residue:
Ligand CMH 4 x CMH

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 39.02Å b: 61.52Å c: 72.8Å
α: 91.8° β: 98.73° γ: 90.01°
R-values:
R R work R free
0.183 0.181 0.224
Expression system: Escherichia coli

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Citations

4 review citations

Recombinant Endolysins as Potential Therapeutics against Antibiotic-Resistant Staphylococcus aureus: Current Status of Research and Novel Delivery Strategies.
Haddad Kashani et al. (2018)
3 more

5 mentions without citation

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.
Vermassen et al. (2019)
4 more

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