期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 430, 期 17, 页码 2677-2687出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2018.06.006
关键词
ribosome translocation; cryo-EM; eEF2; diphthamide; reading-frame maintenance
资金
- French National Research Agency [ANR-15-CE11-0021-01]
- Fondation ARC pour la recherche sur le cancer
- La Fondation pour la Recherche Medicale, France [DBF20160635745]
- European Research Council [294312]
- Russian Government Program of Competitive Growth of Kazan Federal University
- Equipex Equip@Meso project
- @RAction program ANR CryoEM80S [ANR-14-ACHN-0024]
- French National Research Agency
- European Research Council (ERC) [294312] Funding Source: European Research Council (ERC)
- Agence Nationale de la Recherche (ANR) [ANR-14-ACHN-0024] Funding Source: Agence Nationale de la Recherche (ANR)
One of the most critical steps of protein biosynthesis is the coupled movement of mRNA, which encodes genetic information, with tRNAs on the ribosome. In eukaryotes, this process is catalyzed by a conserved G-protein, the elongation factor 2 (eEF2), which carries a unique post-translational modification, called diphthamide, found in all eukaryotic species. Here we present near-atomic resolution cryo-electron microscopy structures of yeast 80S ribosome complexes containing mRNA, tRNA and eEF2 trapped in different GTP-hydrolysis states which provide further structural insights into the role of diphthamide in the mechanism of translation fidelity in eukaryotes. (C) 2018 Elsevier Ltd. All rights reserved.
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