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.
Berisio
Rita
R
Max-Planck-Research Unit for Ribosomal Structure, Hamburg, Germany.
Harms
Joerg
J
Schluenzen
Frank
F
Zarivach
Raz
R
Hansen
Harly A S
HA
Fucini
Paola
P
Yonath
Ada
A
D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D034301:Deinococcus / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism; D024881:Drug Resistance, Bacterial; D004917:Erythromycin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D048628:Ketolides; D018942:Macrolides; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012338:RNA, Ribosomal, 23S / Q000235:genetics / Q000378:metabolism
D000900:Anti-Bacterial Agents; D048628:Ketolides; D018942:Macrolides; D012338:RNA, Ribosomal, 23S; D004917:Erythromycin; C405499:cethromycin; C106791:telithromycin