Browse by author
Lookup NU author(s): Dr Sergey MelnikovORCiD
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
© 2018 Elsevier LtdOne 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.
Author(s): Pellegrino S, Demeshkina N, Mancera-Martinez E, Melnikov S, Simonetti A, Myasnikov A, Yusupov M, Yusupova G, Hashem Y
Publication type: Article
Publication status: Published
Journal: Journal of Molecular Biology
Year: 2018
Volume: 430
Issue: 17
Pages: 2677-2687
Print publication date: 17/08/2018
Online publication date: 07/06/2018
Acceptance date: 04/06/2018
ISSN (print): 0022-2836
ISSN (electronic): 1089-8638
Publisher: Academic Press
URL: https://doi.org/10.1016/j.jmb.2018.06.006
DOI: 10.1016/j.jmb.2018.06.006
PubMed id: 29886014
Altmetrics provided by Altmetric