Cargando…
Investigating the entire course of telithromycin binding to Escherichia coli ribosomes
Applying kinetics and footprinting analysis, we show that telithromycin, a ketolide antibiotic, binds to Escherichia coli ribosomes in a two-step process. During the first, rapidly equilibrated step, telithromycin binds to a low-affinity site (K(T) = 500 nM), in which the lactone ring is positioned...
Autores principales: | Kostopoulou, Ourania N., Petropoulos, Alexandros D., Dinos, George P., Choli-Papadopoulou, Theodora, Kalpaxis, Dimitrios L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3367204/ https://www.ncbi.nlm.nih.gov/pubmed/22362747 http://dx.doi.org/10.1093/nar/gks174 |
Ejemplares similares
-
Changes in the conformation of 5S rRNA cause alterations in principal functions of the ribosomal nanomachine
por: Kouvela, Ekaterini C., et al.
Publicado: (2007) -
Conjugation with polyamines enhances the antibacterial and anticancer activity of chloramphenicol
por: Kostopoulou, Ourania N., et al.
Publicado: (2014) -
Localization of spermine binding sites in 23S rRNA by photoaffinity labeling: parsing the spermine contribution to ribosomal 50S subunit functions
por: Xaplanteri, Maria A., et al.
Publicado: (2005) -
Role of ribosome assembly in Escherichia coli ribosomal RNA degradation
por: Jain, Chaitanya
Publicado: (2018) -
Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites
por: Allemand, F., et al.
Publicado: (2007)