4CT3

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

Summary for 4CT3

Entry DOI	10.2210/pdb4ct3/pdb
Related	4CSH
Descriptor	ORF30/ORF32, CHLORIDE ION, GLYCEROL, ... (8 entities in total)
Functional Keywords	viral protein, peptidoglycan, protease
Biological source	Kayvirus kay
Total number of polymer chains	4
Total formula weight	79598.92
Authors	Sanz-Gaitero, M.,Keary, R.,Garcia-Doval, C.,Coffey, A.,van Raaij, M.J. (deposition date: 2014-03-12, release date: 2014-08-06, Last modification date: 2024-11-20)
Primary citation	Sanz-Gaitero, M.,Keary, R.,Garcia-Doval, C.,Coffey, A.,van Raaij, M.J. Crystal structure of the lytic CHAP(K) domain of the endolysin LysK from Staphylococcus aureus bacteriophage K. Virol. J., 11:133-133, 2014 Cited by PubMed Abstract: Bacteriophages encode endolysins to lyse their host cell and allow escape of their progeny. Endolysins are also active against Gram-positive bacteria when applied from the outside and are thus attractive anti-bacterial agents. LysK, an endolysin from staphylococcal phage K, contains an N-terminal cysteine-histidine dependent amido-hydrolase/peptidase domain (CHAP(K)), a central amidase domain and a C-terminal SH3b cell wall-binding domain. CHAP(K) cleaves bacterial peptidoglycan between the tetra-peptide stem and the penta-glycine bridge. PubMed: 25064136 DOI: 10.1186/1743-422X-11-133 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.69 Å)

Structure validation