ArticleNature structural & molecular biology2022
Structural basis for context-specific inhibition of translation by oxazolidinone antibiotics.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 66 citations in OpenAlex.
- Halting translation by the letter with sequence-selective small molecules.Nature chemical biology · 2026Review
- Sparsomycin inhibits translation through a conserved mechanism across all domains of life.Nucleic acids research · 2026Article
- Structural adaptations for enhanced translation kinetics in evolved ribosomes.Nucleic acids research · 2026Article
- Approaches for Studying Context Specificity of Translation Inhibitor Action.International journal of molecular sciences · 2026Review
- Off-target anti-leukemic effects of antibiotics: mechanisms and therapeutic insights.Cancer chemotherapy and pharmacology · 2026Review
- Simultaneous quantification of linezolid and its metabolites (PNU-142300 and PNU-142586) in oral fluid and capillary blood by UPLC-MS/MS: method validation and clinical application using non-invasive sampling techniques.Journal of translational medicine · 2026Article
- A multi-stage computational pipeline andRSC advances · 2026Article
- Structural adaptations for enhanced translation kinetics in evolved ribosomes.bioRxiv : the preprint server for biology · 2026Article
- Context-dependent translation inhibition as a cancer therapeutic modality.Nature communications · 2026Article
- Structural modification of oxazolidinone antibiotics alters nascent peptide stalling preference and peptide trajectory through the ribosome.bioRxiv : the preprint server for biology · 2026Article
- Structural Analysis of 23S rRNA Methylating Enzyme Cfr Reveals RNA-Binding Determinants for Methylation Regiospecificity and Antibiotic Resistance.ACS infectious diseases · 2026Article
- Discovery and development of a new oxazolidinone with reduced toxicity for the treatment of tuberculosis.Nature medicine · 2026Article
- A low-toxicity linezolid analog has potential for use in all patients with tuberculosis.Nature medicine · 2026Article
- Design, Synthesis and Biological Evaluation of New Oxazolidinone Antimicrobial Agents with Low Monoamine Oxidase A Inhibition.Drug design, development and therapy · 2026Article
- Article
- Synthesis and antibacterial activity of novel benzodioxin-containing oxazolidinones against M. abscessus.Bioorganic & medicinal chemistry letters · 2025Article
- Hybrid Antibiotics Targeting the Bacterial Ribosome.ACS central science · 2025Article
- Structural analysis of 23S rRNA methylating enzyme Cfr reveals RNA binding determinants for methylation regiospecificity and antibiotic resistance.bioRxiv : the preprint server for biology · 2025Article
- Sequence-specific trapping of EF-Tu/glycyl-tRNA complex on the ribosome by bottromycin.bioRxiv : the preprint server for biology · 2025Article
- Redesigning oxazolidinones as carbonic anhydrase inhibitors against vancomycin-resistant enterococci.European journal of medicinal chemistry · 2025Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
The antibiotic linezolid, the first clinically approved member of the oxazolidinone class, inhibits translation of bacterial ribosomes by binding to the peptidyl transferase center. Recent work has demonstrated that linezolid does not inhibit peptide bond formation at all sequences but rather acts in a context-specific manner, namely when alanine occupies the penultimate position of the nascent chain. However, the molecular basis for context-specificity has not been elucidated. Here we show that the second-generation oxazolidinone radezolid also induces stalling with a penultimate alanine, and we determine high-resolution cryo-EM structures of linezolid- and radezolid-stalled ribosome complexes to explain their mechanism of action. These structures reveal that the alanine side chain fits within a small hydrophobic crevice created by oxazolidinone, resulting in improved ribosome binding. Modification of the ribosome by the antibiotic resistance enzyme Cfr disrupts stalling due to repositioning of the modified nucleotide. Together, our findings provide molecular understanding for the context-specificity of oxazolidinones.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.