Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation
Copyright policy )Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation
An 11.7-A-resolution cryo-EM map of the yeast 80S.eEF2 complex in the presence of the antibiotic sordarin was interpreted in molecular terms, revealing large conformational changes within eEF2 and the 80S ribosome, including a rearrangement of the functionally important ribosomal intersubunit bridges. Sordarin positions domain III of eEF2 so that it can interact with the sarcin-ricin loop of 25S rRNA and protein rpS23 (S12p). This particular conformation explains the inhibitory action of sordarin and suggests that eEF2 is stalled on the 80S ribosome in a conformation that has similarities with the GTPase activation state. A ratchet-like subunit rearrangement (RSR) occurs in the 80S.eEF2.sordarin complex that, in contrast to Escherichia coli 70S ribosomes, is also present in vacant 80S ribosomes. A model is suggested, according to which the RSR is part of a mechanism for moving the tRNAs during the translocation reaction.
- State University of New York at Potsdam United States
- Aarhus University Denmark
- The University of Texas System United States
- Humboldt-Universität zu Berlin Germany
- Spanish National Research Council Spain
Models, Molecular, Antifungal Agents, Movement, Cryoelectron Microscopy, Saccharomyces cerevisiae, Crystallography, X-Ray, RNA Transport, Protein Structure, Tertiary, Protein Subunits, Indenes, Peptide Elongation Factor 2, RNA, Transfer, Nucleic Acid Conformation, Protein Structure, Quaternary, Ribosomes, Protein Binding
Models, Molecular, Antifungal Agents, Movement, Cryoelectron Microscopy, Saccharomyces cerevisiae, Crystallography, X-Ray, RNA Transport, Protein Structure, Tertiary, Protein Subunits, Indenes, Peptide Elongation Factor 2, RNA, Transfer, Nucleic Acid Conformation, Protein Structure, Quaternary, Ribosomes, Protein Binding
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