Crystal structure of the lytic CHAPK domain of the endolysin LysK from Staphylococcus aureus bacteriophage K

[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...

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Detalhes bibliográficos
Autores: Sanz-Gaitero, Marta, Keary, Ruth, García-Doval, Carmela, Coffey, Aidan, van Raaij, Mark J.
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2014
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositório:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/125903
Acesso em linha:http://hdl.handle.net/10261/125903
Access Level:Acceso aberto
Palavra-chave:Bacteriophage
Calcium
Crystallography
Endolysin
Peptidoglycan
Protease
Staphylococcus
Zinc
Descrição
Resumo:[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 (CHAPK), a central amidase domain and a C-terminal SH3b cell wall-binding domain. CHAPK cleaves bacterial peptidoglycan between the tetra-peptide stem and the penta-glycine bridge.

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