Keywords: Cethromycin, Erythromycin, Ketolide, Macrolide, Telithromycin, Antibiotic Resistance, Article, Bacterium Mutant, Binding Site, Crystal Structure, Deinococcus Radiodurans, Drug Mechanism, Drug Protein Binding, Drug Structure, Nonhuman, Priority Journal, Protein Domain, Protein Interaction, Ribosome, Anti-Bacterial Agents, Crystallization, Crystallography, X-Ray, Drug Resistance, Models, Molecular, Molecular Sequence Data, 23s, Bacteria (microorganisms), Posibacteria,
Affiliations: *** IBB - CNR ***
Max-Planck-Res. U. Ribosomal Struct., Hamburg, Germany
Max-Planck-Inst. for Molec. Genet., Berlin, Germany
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Inst. of Biostructure and Bioimaging, CNR, Naples, Italy
References: Not available.
Structural insight into the antibiotic action of telithromycin against resistant mutants
The crystal structure of the ketolide telithromycin bound to the Deinococcus radiodurans large ribosomal subunit shows that telithromycin blocks the ribosomal exit tunnel and interacts with domains II and V of the 23S RNA. Comparisons to other clinically relevant macrolides provided structural insights into its enhanced activity against macrolide-resistant strains.
Structural insight into the antibiotic action of telithromycin against resistant mutants
No results.
Structural insight into the antibiotic action of telithromycin against resistant mutants