bioRxivBiochemistryPreprint
Orthoformimycin inhibits translation elongation by displacing the A-site tRNA and preventing peptide bond formation
A. Schedlbauer, T. Kaminishi, A. Fabbretti, P. Milon, X. Han, B. Ochoa-Lizarralde, R. Capuni, C. O. Gualerzi, S. R. Connell, P. Fucini
Abstract
The ribosome is a major target for antibiotics owing to its essential cellular role in protein synthesis. Structural analysis of ribosome-antibiotic complexes provides insight into the molecular basis for their inhibitory action and highlights possible avenues to improve their potential or overcome existing resistance mechanisms. Here we use X-ray crystallography and pre-steady state kinetics to detail the inhibitory mechanism of the antimicrobial on the large ribosomal subunit.
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Characterization of a potential antibiotic target site on the ribosome
Michael Golstein, Yang Wang, … Paul C. Whitford·bioRxiv·May 2, 2025
- Structural basis for the context-specific action of classic peptidyl transferase inhibitors.
Egor A. Syroegin, Laurin Flemmich, … Yury S. Polikanov·Nature Structural & Molecular BiologyPeer-reviewed·Feb 1, 2022
- Structural basis for context-specific inhibition of translation by oxazolidinone antibiotics
K. Tsai, V. Stojkovic, … D. Galonic Fujimori·bioRxiv·Aug 10, 2021
- Perturbation of ribosomal subunits dynamics by inhibitors of tRNA translocation
Riccardo Belardinelli, Heena Sharma, … Marina V. Rodnina·RNAPeer-reviewed·Jun 11, 2021
- Structural insights into context-dependent inhibitory mechanisms of chloramphenicol in cells
L. Xue, C. M. T. Spahn, … J. Mahamid·bioRxiv·Jun 7, 2023
- Structural insights into context-specific inhibition of bacterial translation by macrolides
Egor A. Syroegin, Elena V. Aleksandrova, … Yury S. Polikanov·Nature CommunicationsPeer-reviewed·Nov 3, 2025