Structural insight into the antibiotic action of telithromycin against resistant mutants

J Bacteriol. 2003 Jul;185(14):4276-9. doi: 10.1128/JB.185.14.4276-4279.2003.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology*
  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Deinococcus / drug effects*
  • Deinococcus / genetics
  • Deinococcus / metabolism
  • Drug Resistance, Bacterial*
  • Erythromycin / analogs & derivatives*
  • Erythromycin / chemistry
  • Erythromycin / metabolism
  • Erythromycin / pharmacology
  • Humans
  • Ketolides*
  • Macrolides*
  • Models, Molecular
  • Molecular Sequence Data
  • RNA, Ribosomal, 23S / genetics
  • RNA, Ribosomal, 23S / metabolism

Substances

  • Anti-Bacterial Agents
  • Ketolides
  • Macrolides
  • RNA, Ribosomal, 23S
  • Erythromycin
  • cethromycin
  • telithromycin

Associated data

  • PDB/!P9X