ArticleJournal of molecular biology2012
The antibiotic thermorubin inhibits protein synthesis by binding to inter-subunit bridge B2a of the ribosome.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Annulation Methods toward the Total Synthesis of Thermorubin: Construction of the AB and BCD Ring Systems.The Journal of organic chemistry · 2025Article
- Hibernating ribosomes as drug targets?Frontiers in microbiology · 2024Review
- Antibiotic thermorubin tethers ribosomal subunits and impedes A-site interactions to perturb protein synthesis in bacteria.Nature communications · 2023Article
- Isolation and screening ofIranian journal of microbiology · 2023Article
- Insights into the molecular mechanism of translation inhibition by the ribosome-targeting antibiotic thermorubin.Nucleic acids research · 2023Article
- CBD resistantFrontiers in medicine · 2023Article
- Context-sensitivity of isosteric substitutions of non-Watson-Crick basepairs in recurrent RNA 3D motifs.Nucleic acids research · 2021Article
- Perturbation of ribosomal subunit dynamics by inhibitors of tRNA translocation.RNA (New York, N.Y.) · 2021Article
- Structure of the 70S Ribosome from the Human Pathogen Acinetobacter baumannii in Complex with Clinically Relevant Antibiotics.Structure (London, England : 1993) · 2020Article
- Enhanced efficacy of chemically modified curcumin in experimental periodontitis: systemic implications.Journal of experimental pharmacology · 2019Article
- Ribosome-Targeting Antibiotics: Modes of Action, Mechanisms of Resistance, and Implications for Drug Design.Annual review of biochemistry · 2018Review
- Exploring allosteric communication in multiple states of the bacterial ribosome using residue network analysis.Turkish journal of biology = Turk biyoloji dergisi · 2018Article
- The development of peptide ligands that target helix 69 rRNA of bacterial ribosomes.Bioorganic & medicinal chemistry · 2016Article
- Bacterial Protein Synthesis as a Target for Antibiotic Inhibition.Cold Spring Harbor perspectives in medicine · 2016Review
- Ribosomal Antibiotics: Contemporary Challenges.Antibiotics (Basel, Switzerland) · 2016Review
- Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition.Nucleic acids research · 2016Article
- tRNAs as antibiotic targets.International journal of molecular sciences · 2014Review
- Article
- Ribosome-targeting antibiotics and mechanisms of bacterial resistance.Nature reviews. Microbiology · 2014Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Thermorubin is a small-molecule inhibitor of bacterial protein synthesis, but relatively little is known about the molecular mechanism by which it blocks translation. The structure of the complex between thermorubin and the 70S ribosome from Thermus thermophilus reported here shows that thermorubin interacts with the ribosome in a way that is distinct from any other known class of ribosome inhibitor. Though it is structurally similar to tetracycline, it binds to the ribosome at an entirely different location-the interface between the small and large subunits that is formed by inter-subunit bridge B2a. This region of the ribosome is known to play a role in the initiation of translation, and thus, the binding site we observe is consistent with evidence suggesting that thermorubin inhibits the initiation stage of protein synthesis. The binding of thermorubin induces a rearrangement of two bases on helix 69 of the 23S rRNA, and presumably, this rearrangement blocks the binding of an A-site tRNA, thereby inhibiting peptide bond formation. Due in part to its low solubility in aqueous media, thermorubin has not been used clinically, although it is a potent antibacterial agent with low toxicity (Therapeutic Index>200). The interactions between thermorubin and the ribosome, as well as its adjacency to the observed binding sites of three other antibiotic classes, may enable the design of novel derivatives that share thermorubin's mode of action but possess improved pharmacodynamic properties.
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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.