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

Research team article "Ribosome, Bacteria and Stress" by Reynald Gillet published in Nucleic Acids Research

The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors
Kevin Macé, Emmanuel Giudice, Sophie Chat and Reynald Gillet
Nucleic Acids Research, gky081, https://doi.org/10.1093/nar/gky081

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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