Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding
Author:
Funder
EC | Horizon 2020
Virus-X project: Viral Metagenomics for Innovation Value
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-018-37417-6.pdf
Reference44 articles.
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2. Nelson, D. C. et al. Endolysins as antimicrobials. Adv Virus Res 83, 299–365, https://doi.org/10.1016/B978-0-12-394438-2.00007-4 (2012).
3. Chakravorty, D., Khan, M. F. & Patra, S. Multifactorial level of extremostability of proteins: can they be exploited for protein engineering? Extremophiles 21, 419–444, https://doi.org/10.1007/s00792-016-0908-9 (2017).
4. Dumorné, K., Córdova, D. C., Astorga-Eló, M. & Renganathan, P. Extremozymes: A Potential Source for Industrial Applications. J Microbiol Biotechnol 27, 649–659, https://doi.org/10.4014/jmb.1611.11006 (2017).
5. Plotka, M. et al. Biochemical Characterization and Validation of a Catalytic Site of a Highly Thermostable Ts2631 Endolysin from the Thermus scotoductus Phage vB_Tsc2631. PLoS One 10, e0137374, https://doi.org/10.1371/journal.pone.0137374 (2015).
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