ArticleNucleic acids research2018
The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis.Nature communications · 2025Article
- Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome.Nucleic acids research · 2023Article
- High-level in vitro resistance to gentamicin acquired in a stepwise manner in Neisseria gonorrhoeae.The Journal of antimicrobial chemotherapy · 2023Article
- Hyper-swivel head domain motions are required for complete mRNA-tRNA translocation and ribosome resetting.Nucleic acids research · 2022Article
- Modeling the ribosome as a bipartite graph.PloS one · 2022Article
- Structural mechanism of GTPase-powered ribosome-tRNA movement.Nature communications · 2021Article
- Global reprogramming of virulence and antibiotic resistance inThe Journal of biological chemistry · 2020Article
- Structural insights into mammalian mitochondrial translation elongation catalyzed by mtEFG1.The EMBO journal · 2020Article
- Structural basis of elongation factor 2 switching.Current research in structural biology · 2020Article
- An Allosteric Network for Spliceosome Activation Revealed by High-Throughput Suppressor Analysis inGenetics · 2019Article
- Time-Course Proteomic Analysis ofPolymers · 2019Article
- Ribosome Structure, Function, and Early Evolution.International journal of molecular sciences · 2018Review
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4 authors.
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Abstract
During translation's elongation cycle, elongation factor G (EF-G) promotes messenger and transfer RNA translocation through the ribosome. Until now, the structures reported for EF-G-ribosome complexes have been obtained by trapping EF-G in the ribosome. These results were based on use of non-hydrolyzable guanosine 5'-triphosphate (GTP) analogs, specific inhibitors or a mutated EF-G form. Here, we present the first cryo-electron microscopy structure of EF-G bound to ribosome in the absence of an inhibitor. The structure reveals a natural conformation of EF-G·GDP in the ribosome, with a previously unseen conformation of its third domain. These data show how EF-G must affect translocation, and suggest the molecular mechanism by which fusidic acid antibiotic prevents the release of EF-G after GTP hydrolysis.
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