title: Crystallization of the CHAP domain of the endolysin from Staphylococcus aureus bacteriophage K.
abstract: CHAP(K) is the N-terminal cysteine, histidine-dependent amidohydrolase/peptidase domain (CHAP domain) of the Staphylococcus aureus bacteriophage K endolysin LysK. It is formed from the first 165 residues of LysK and functions by cleaving specific peptidoglycan peptide bonds, causing bacterial lysis. CHAP(K) can lyse S. aureus when applied exogenously, making it a good candidate for the treatment of multidrug-resistant Staphylococcus aureus infections. Here, the crystallization of CHAP(K) and the collection of native and derivative data to high resolution, which allowed structure solution, are reported. The structure may help to elucidate the mechanism of action and in the design of chimeric proteins or mutants with improved antibacterial activity.
authors: Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Calle Darwin 3, 28049 Madrid, Spain.
authors: Marta
authors: M
authors: Sanz-Gaitero
authors: Ruth
authors: R
authors: Keary
authors: Carmela
authors: C
authors: Garcia-Doval
authors: Aidan
authors: A
authors: Coffey
authors: Mark J
authors: MJ
authors: van Raaij
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001435:Bacteriophages / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013211:Staphylococcus aureus / Q000821:virology; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D014764:Viral Proteins; D000581:Amidohydrolases
keywords: CHAP domain; Staphylococcus aureus; endolysin