Cargando…
Crystal structure and functional analysis of mycobacterial erythromycin resistance methyltransferase Erm38 reveals its RNA-binding site
Erythromycin resistance methyltransferases (Erms) confer resistance to macrolide, lincosamide, and streptogramin antibiotics in Gram-positive bacteria and mycobacteria. Although structural information for ErmAM, ErmC, and ErmE exists from Gram-positive bacteria, little is known about the Erms in myc...
Autores principales: | Goh, Boon Chong, Xiang, Xinyu, Lescar, Julien, Dedon, Peter C. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8844858/ https://www.ncbi.nlm.nih.gov/pubmed/35007529 http://dx.doi.org/10.1016/j.jbc.2022.101571 |
Ejemplares similares
-
Three critical regions of the erythromycin resistance methyltransferase, ErmE, are required for function supporting a model for the interaction of Erm family enzymes with substrate rRNA
por: Sharkey, Rory E., et al.
Publicado: (2022) -
ErmF and ereD Are Responsible for Erythromycin Resistance in Riemerella anatipestifer
por: Xing, Linlin, et al.
Publicado: (2015) -
Crystal structure of ErmE - 23S rRNA methyltransferase in macrolide resistance
por: Stsiapanava, Alena, et al.
Publicado: (2019) -
Translational Attenuation Mechanism of ErmB Induction by Erythromycin Is Dependent on Two Leader Peptides
por: Wang, Shasha, et al.
Publicado: (2021) -
16-membered ring macrolides and erythromycin induce ermB expression by different mechanisms
por: He, Weizhi, et al.
Publicado: (2022)