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

Structural insight into the antibiotic action of telithromycin against resistant mutants

Rita Berisio  1 , Joerg Harms, Frank Schluenzen, Raz Zarivach, Harly A S Hansen, Paola Fucini, Ada Yonath
Affiliations

Structural insight into the antibiotic action of telithromycin against resistant mutants

Rita Berisio et al. J Bacteriol. 2003 Jul.

Erratum in

  • J Bacteriol. 2003 Aug;185(16):5027

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.

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Figures

FIG. 1.
FIG. 1.
(A) Chemical structures of the macrolide erythromycin and the ketolides telithromycin and ABT-773; (B) view into the D50S tunnel with a bound telithromycin molecule (red).
FIG. 2.
FIG. 2.
(A and B) Stereo views of a telithromycin omit electron-density-map (A) and its binding site (B); (C) two-dimensional sketch of telithromycin interactions with D50S; (D) superposition of the positions of telithromycin (gold), ABT-773 (purple) (14), and erythromycin (green) (13) in D50S; (E) view of telithromycin along its extension arm showing its stacking interactions with the groove in domain II.
See this image and copyright information in PMC

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