Sanz-Gaitero Marta, Keary Ruth, Garcia-Doval Carmela, Coffey Aidan, van Raaij Mark J
Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Calle Darwin 3, 28049 Madrid, Spain.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1393-6. doi: 10.1107/S1744309113030133. Epub 2013 Nov 29.
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.
CHAP(K)是金黄色葡萄球菌噬菌体K溶菌酶LysK的N端半胱氨酸、组氨酸依赖性酰胺水解酶/肽酶结构域（CHAP结构域）。它由LysK的前165个残基组成，通过切割特定的肽聚糖肽键发挥作用，导致细菌裂解。当外源性应用时，CHAP(K)可裂解金黄色葡萄球菌，使其成为治疗多重耐药金黄色葡萄球菌感染的良好候选物。本文报道了CHAP(K)的结晶以及高分辨率天然和衍生数据的收集，这些数据有助于解析其结构。该结构可能有助于阐明其作用机制，并用于设计具有改善抗菌活性的嵌合蛋白或突变体。
