Crystallization Of The CHAP Domain Of The Endolysin From Staphylococcus Aureus Bacteriophage K

Authors

Marta Sanz-Gaitero, Centro Nacional de Biotecnología
Ruth Keary, Department of Biological Sciences, Cork Institute of Technology
Carmela Garcia-Doval, Centro Nacional de Biotecnología
Aidan Coffey, Department of Biological Sciences, Cork Institute of Technology, Bishopstown, Cork, IrelandFollow
Mark J. van Raaij, Centro Nacional de Biotecnología

Document Type

Article

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

Disciplines

Biology

Publication Details

Acta Crystallographica Section F Structural Biology and Crystallization Communications.

Abstract

CHAPK 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. CHAPK 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 CHAPK 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.

Recommended Citation

Sanz-Gaitero, M. et al., 2013. Crystallization of the CHAP domain of the endolysin fromStaphylococcus aureusbacteriophage K. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 69(12), pp.1393–1396. Available at: http://dx.doi.org/10.1107/S1744309113030133.