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Structural insight into the antibiotic action of telithromycin against resistant mutants (vol 185, pg 4276, 2003)

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50097

Berisio,  Rita
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

Harms,  Joerg
Max Planck Society;

Schluenzen,  Frank
Max Planck Society;

Hansen,  Harly A. S.
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50160

Fucini,  Paola
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

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Citation

Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H. A. S., Fucini, P., et al. (2003). Structural insight into the antibiotic action of telithromycin against resistant mutants (vol 185, pg 4276, 2003). Journal of Bacteriology, 185(14), 4276-4279.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8A06-4
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.