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
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / metabolism
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Anti-Bacterial Agents / pharmacology*
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Binding Sites
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Crystallization
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Crystallography, X-Ray
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Deinococcus / drug effects*
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Deinococcus / genetics
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Deinococcus / metabolism
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Drug Resistance, Bacterial*
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Erythromycin / analogs & derivatives*
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Erythromycin / chemistry
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Erythromycin / metabolism
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Erythromycin / pharmacology
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Humans
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Ketolides*
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Macrolides*
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Models, Molecular
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Molecular Sequence Data
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RNA, Ribosomal, 23S / genetics
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RNA, Ribosomal, 23S / metabolism
Substances
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Anti-Bacterial Agents
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Ketolides
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Macrolides
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RNA, Ribosomal, 23S
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Erythromycin
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cethromycin
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telithromycin