期刊
EMBO JOURNAL
卷 23, 期 5, 页码 1008-1019出版社
WILEY
DOI: 10.1038/sj.emboj.7600102
关键词
cryo-EM; eEF2; 80S ribosome; sordarin; tRNA translocation
资金
- NIGMS NIH HHS [R01 GM060635, R01 GM55440, R37 GM029169, R01 GM60635, R37 GM29169, R01 GM055440] Funding Source: Medline
An 11.7-Angstrom-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.
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