Crystallization of the CHAP domain of the endolysin from Staphylococcus aureus bacteriophage K. Issue 12 (1st December 2013)

• Record Type: Journal Article
• Authors: Sanz‐Gaitero, Marta; Keary, Ruth; Garcia‐Doval, Carmela; Coffey, Aidan; van Raaij, Mark J.
• Is Part Of: Acta crystallographica. Volume 69:Issue 12(2013:Dec.)
• Page Start: 1393
• Page End: 1396
• Publication Date: 2013-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113030133
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>CHAP_K is the N‐terminal cysteine, histidine‐dependent amidohydrolase/peptidase domain (CHAP domain) of the <italic>Staphylococcus aureus</italic> 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 <italic>S. aureus</italic> when applied exogenously, making it a good candidate for the treatment of multidrug‐resistant <italic>Staphylococcus aureus</italic> 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.</p> </abstract>