Structural analysis of kasugamycin inhibition of translation
Copyright policy )Structural analysis of kasugamycin inhibition of translation
The prokaryotic ribosome is an important target of antibiotic action. We determined the X-ray structure of the aminoglycoside kasugamycin (Ksg) in complex with the Escherichia coli 70S ribosome at 3.5-A resolution. The structure reveals that the drug binds within the messenger RNA channel of the 30S subunit between the universally conserved G926 and A794 nucleotides in 16S ribosomal RNA, which are sites of Ksg resistance. To our surprise, Ksg resistance mutations do not inhibit binding of the drug to the ribosome. The present structural and biochemical results indicate that inhibition by Ksg and Ksg resistance are closely linked to the structure of the mRNA at the junction of the peptidyl-tRNA and exit-tRNA sites (P and E sites).
- Lawrence Berkeley National Laboratory United States
- University of California, San Francisco United States
- Brown University United States
- United States Department of Agriculture United States
- Miami University United States
Models, Molecular, Binding Sites, Base Sequence, Molecular Sequence Data, Templates, Genetic, Anti-Bacterial Agents, Protein Structure, Tertiary, RNA, Bacterial, Structure-Activity Relationship, Aminoglycosides, Protein Biosynthesis, Mutation, Escherichia coli, RNA, Messenger, Ribosomes
Models, Molecular, Binding Sites, Base Sequence, Molecular Sequence Data, Templates, Genetic, Anti-Bacterial Agents, Protein Structure, Tertiary, RNA, Bacterial, Structure-Activity Relationship, Aminoglycosides, Protein Biosynthesis, Mutation, Escherichia coli, RNA, Messenger, Ribosomes
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