The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors

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.
Document type :
Journal articles
Complete list of metadatas

Cited literature [44 references]  Display  Hide  Download

https://hal-univ-rennes1.archives-ouvertes.fr/hal-01795396
Contributor : Laurent Jonchère <>
Submitted on : Thursday, July 18, 2019 - 1:16:52 PM
Last modification on : Saturday, July 20, 2019 - 1:17:27 AM

File

gky081.pdf
Publisher files allowed on an open archive

Identifiers

Citation

Kevin Macé, Emmanuel Giudice, Sophie Chat, Reynald Gillet. The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors. Nucleic Acids Research, Oxford University Press, 2018, 46 (6), pp.3211-3217. ⟨10.1093/nar/gky081⟩. ⟨hal-01795396⟩

Share

Metrics

Record views

32

Files downloads

36