5ot7

Publication Abstract from PubMed

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.

The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors.,Mace K, Giudice E, Chat S, Gillet R Nucleic Acids Res. 2018 Feb 2. pii: 4835058. doi: 10.1093/nar/gky081. PMID:29408956^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.