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-Structure paper
| Title | The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors. |
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| Journal, issue, pages | Nucleic Acids Res, Vol. 46, Issue 6, Page 3211-3217, Year 2018 |
| Publish date | Apr 6, 2018 |
 Authors | Kevin Macé / Emmanuel Giudice / Sophie Chat / Reynald Gillet /  |
| PubMed 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 ...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. |
 External links | Nucleic Acids Res / PubMed:29408956 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.8 Å |
| Structure data | |
| Chemicals |  ChemComp-MG:  ChemComp-ZN:  ChemComp-GDP: |
| Source |
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 Keywords |  RIBOSOME / Elongation factor G / Translation / Translocation |
