Cargando…
Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding
To escape from hosts after completing their life cycle, bacteriophages often use endolysins, which degrade bacterial peptidoglycan. While mesophilic phages have been extensively studied, their thermophilic counterparts are not well characterized. Here, we present a detailed analysis of the structure...
Autores principales: | Plotka, Magdalena, Sancho-Vaello, Enea, Dorawa, Sebastian, Kaczorowska, Anna-Karina, Kozlowski, Lukasz P., Kaczorowski, Tadeusz, Zeth, Kornelius |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6361986/ https://www.ncbi.nlm.nih.gov/pubmed/30718611 http://dx.doi.org/10.1038/s41598-018-37417-6 |
Ejemplares similares
-
Ts2631 Endolysin from the Extremophilic Thermus scotoductus Bacteriophage vB_Tsc2631 as an Antimicrobial Agent against Gram-Negative Multidrug-Resistant Bacteria
por: Plotka, Magdalena, et al.
Publicado: (2019) -
Biochemical Characterization and Validation of a Catalytic Site of a Highly Thermostable Ts2631 Endolysin from the Thermus scotoductus Phage vB_Tsc2631
por: Plotka, Magdalena, et al.
Publicado: (2015) -
AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase
por: Jasilionis, Andrius, et al.
Publicado: (2023) -
Whole-body Vibration Exposure Experienced by Dumper Operators in Opencast Mining According to ISO 2631-1:1997 and ISO 2631-5:2004: A Case Study
por: Prajapati, Shivkumar Shrinarayan, et al.
Publicado: (2020) -
The reconstruction of 2,631 draft metagenome-assembled genomes from the global oceans
por: Tully, Benjamin J., et al.
Publicado: (2018)