Structural bases of peptidoglycan recognition by lysostaphin SH3b domain
Author:
Funder
Fundacja na rzecz Nauki Polskiej
Ministry of Science and Higher Education | Narodowe Centrum Badań i Rozwoju
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-42435-z.pdf
Reference59 articles.
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2. Buist, G., Steen, A., Kok, J. & Kuipers, O. R. LysM, a widely distributed protein motif for binding to (peptido)glycans. Molecular microbiology 68, 838–847, https://doi.org/10.1111/j.1365-2958.2008.06211.x (2008).
3. Hermoso, J. A. et al. Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. Structure 11, 1239–1249 (2003).
4. Donovan, D. M. & Foster-Frey, J. LambdaSa2 prophage endolysin requires Cpl-7-binding domains and amidase-5 domain for antimicrobial lysis of streptococci. FEMS microbiology letters 287, 22–33, https://doi.org/10.1111/j.1574-6968.2008.01287.x (2008).
5. Becker, S. C., Foster-Frey, J., Stodola, A. J., Anacker, D. & Donovan, D. M. Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain. Gene 443, 32–41, https://doi.org/10.1016/j.gene.2009.04.023 (2009).
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