Related Experiment Video
Updated: Apr 18, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 25, 2011
Bactobolin A binds to a site on the 70S ribosome distinct from previously seen antibiotics
Alexey Amunts1, Karol Fiedorczuk1, Thao T Truong2
1MRC Laboratory of Molecular Biology, Cambridge CB20QH, UK.
Abstract:
The ribosome is the target of a large number of antibiotics. Here, we report a 3.4-Å-resolution crystal structure of bactobolin A bound to 70S ribosome-tRNA complex. The antibiotic binds at a previously unseen site in the 50S subunit and displaces tRNA bound at the P-site. It thus likely has a similar mechanism of action as blasticidin S despite binding to a different site. The structure also rationalizes previously identified resistance mutations.
Related Concept Videos
Inhibitors of Bacterial Protein Synthesis
Inhibitors of Gram-positive Cell Wall Synthesis
Mechanism of Antibiotic Resistance in MRSA
Types of RNA
Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse functions and can be broadly classified as protein-coding or non-coding RNA. Non-coding RNAs play important roles in the regulation of gene expression in response to developmental and environmental changes. Non-coding RNAs in prokaryotes can be manipulated to develop more effective antibacterial drugs for human or animal use.
RNA...
Clinical Significance of Antibiotic Resistance
Inhibitors of Bacterial DNA Synthesis

