ArticleNucleic acids research2022
Structural basis for the inability of chloramphenicol to inhibit peptide bond formation in the presence of A-site glycine.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Sparsomycin inhibits translation through a conserved mechanism across all domains of life.Nucleic acids research · 2026Article
- Structural insights into context-specific inhibition of bacterial translation by macrolides.Nature communications · 2025Article
- Sequence-specific trapping of EF-Tu/glycyl-tRNA complex on the ribosome by bottromycin.bioRxiv : the preprint server for biology · 2025Article
- Mechanism of release factor-mediated peptidyl-tRNA hydrolysis on the ribosome.Science (New York, N.Y.) · 2025Article
- Structural insights into context-dependent inhibitory mechanisms of chloramphenicol in cells.Nature structural & molecular biology · 2025Article
- Toxic small alarmone synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAScience advances · 2024Article
- Activity, structure, and diversity of Type II proline-rich antimicrobial peptides from insects.EMBO reports · 2024Article
- Chloramphenicol Interferes with 50S Ribosomal Subunit Maturation via Direct and Indirect Mechanisms.Biomolecules · 2024Article
- Berberine analog of chloramphenicol exhibits a distinct mode of action and unveils ribosome plasticity.Structure (London, England : 1993) · 2024Article
- A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis.Nucleic acids research · 2024Article
- Toxic Small Alarmone Synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAbioRxiv : the preprint server for biology · 2024Article
- Structural basis of Cfr-mediated antimicrobial resistance and mechanisms to evade it.Nature chemical biology · 2024Article
- An antibiotic preorganized for ribosomal binding overcomes antimicrobial resistance.Science (New York, N.Y.) · 2024Article
- Development of 2nd generation aminomethyl spectinomycins that overcome native efflux inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Synthesis of Peptidyl-tRNA Mimics for Structural Biology Applications.Accounts of chemical research · 2023Review
- Structural basis for translation inhibition by the glycosylated drosocin peptide.Nature chemical biology · 2023Article
- Genome-encoded ABCF factors implicated in intrinsic antibiotic resistance in Gram-positive bacteria: VmlR2, Ard1 and CplR.Nucleic acids research · 2023Article
- Insights into the molecular mechanism of translation inhibition by the ribosome-targeting antibiotic thermorubin.Nucleic acids research · 2023Article
- Conjugates of Chloramphenicol Amine and Berberine as Antimicrobial Agents.Antibiotics (Basel, Switzerland) · 2022Article
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3 authors at 1 institution in 1 country.
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Abstract
Ribosome serves as a universal molecular machine capable of synthesis of all the proteins in a cell. Small-molecule inhibitors, such as ribosome-targeting antibiotics, can compromise the catalytic versatility of the ribosome in a context-dependent fashion, preventing transpeptidation only between particular combinations of substrates. Classic peptidyl transferase center inhibitor chloramphenicol (CHL) fails to inhibit transpeptidation reaction when the incoming A site acceptor substrate is glycine, and the molecular basis for this phenomenon is unknown. Here, we present a set of high-resolution X-ray crystal structures that explain why CHL is unable to inhibit peptide bond formation between the incoming glycyl-tRNA and a nascent peptide that otherwise is conducive to the drug action. Our structures reveal that fully accommodated glycine residue can co-exist in the A site with the ribosome-bound CHL. Moreover, binding of CHL to a ribosome complex carrying glycyl-tRNA does not affect the positions of the reacting substrates, leaving the peptide bond formation reaction unperturbed. These data exemplify how small-molecule inhibitors can reshape the A-site amino acid binding pocket rendering it permissive only for specific amino acid residues and rejective for the other substrates extending our detailed understanding of the modes of action of ribosomal antibiotics.
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