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Journal Articles Nucleic Acids Research Year : 2018

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.

Domains

Genetics
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Dates and versions

hal-01795396 , version 1 (18-07-2019)

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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, 2018, 46 (6), pp.3211-3217. ⟨10.1093/nar/gky081⟩. ⟨hal-01795396⟩
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