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Article

Crystal structure of the lytic CHAP(K) domain of the endolysin LysK from Staphylococcus aureus bacteriophage K.

Virology journal - 26 Jul 2014

Sanz-Gaitero Marta, Keary Ruth, Garcia-Doval Carmela, Coffey Aidan, van Raaij Mark J

Abstract excerpt

BACKGROUND: 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...

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Identifiers

PMID: 25064136
DOI: 10.1186/1743-422X-11-133
PMCID: PMC4126393

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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