ArticleScientific reports2020
Cryo-electron microscopy structure of the 70S ribosome from Enterococcus faecalis.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- Structural characterization of ribosome recycling and fusidic acid inhibition in Staphylococcus aureus.Nucleic acids research · 2026Article
- Redesigning oxazolidinones as carbonic anhydrase inhibitors against vancomycin-resistant enterococci.European journal of medicinal chemistry · 2025Article
- Unveiling the structural and functional implications of uncharacterized NSPs and variations in the molecular toolkit across arteriviruses.NAR genomics and bioinformatics · 2025Article
- Creation of a macrolide antibiotic against non-tuberculousScience advances · 2025Article
- Interactions between terminal ribosomal RNA helices stabilize theRNA (New York, N.Y.) · 2023Article
- Ratchet, swivel, tilt and roll: a complete description of subunit rotation in the ribosome.Nucleic acids research · 2023Article
- Article
- Phage-Related Ribosomal Proteases (Prps): Discovery, Bioinformatics, and Structural Analysis.Antibiotics (Basel, Switzerland) · 2022Article
- Structural basis for PoxtA-mediated resistance to phenicol and oxazolidinone antibiotics.Nature communications · 2022Article
- Annealing synchronizes the 70Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Maturation of 23S rRNA includes removal of helix H1 in many bacteria.RNA biology · 2021Article
- Mechanisms of catalytic RNA molecules.Biochemical Society transactions · 2021Review
- Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens.Nature communications · 2021Article
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9 authors.
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Abstract
Enterococcus faecalis is a gram-positive organism responsible for serious infections in humans, but as with many bacterial pathogens, resistance has rendered a number of commonly used antibiotics ineffective. Here, we report the cryo-EM structure of the E. faecalis 70S ribosome to a global resolution of 2.8 Å. Structural differences are clustered in peripheral and solvent exposed regions when compared with Escherichia coli, whereas functional centres, including antibiotic binding sites, are similar to other bacterial ribosomes. Comparison of intersubunit conformations among five classes obtained after three-dimensional classification identifies several rotated states. Large ribosomal subunit protein bL31, which forms intersubunit bridges to the small ribosomal subunit, assumes different conformations in the five classes, revealing how contacts to the small subunit are maintained throughout intersubunit rotation. A tRNA observed in one of the five classes is positioned in a chimeric pe/E position in a rotated ribosomal state. The 70S ribosome structure of E. faecalis now extends our knowledge of bacterial ribosome structures and may serve as a basis for the development of novel antibiotic compounds effective against this pathogen.
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