6GQB

Cryo-EM reconstruction of yeast 80S ribosome in complex with mRNA, tRNA and eEF2 (GDP+AlF4/sordarin)

This is a non-PDB format compatible entry.

Summary for 6GQB

• Entry DOI: 10.2210/pdb6gqb/pdb
• Related: 6GQ1 6GQV
• EMDB information: 0047 0048 0049 0055
• Descriptor: Saccharomyces cerevisiae S288C 35S pre-ribosomal RNA (RDN37-1), miscRNA, 60S ribosomal protein L6-A, 60S ribosomal protein L7-A, ... (88 entities in total)
• Functional Keywords: eukaryotic 80s ribosome, eef2, translation fidelity, diphthamide, ribosome
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 84
• Total formula weight: 3192520.80

Authors

Pellegrino, S.,Yusupov, M.,Yusupova, G.,Hashem, Y. (deposition date: 2018-06-07, release date: 2018-07-11, Last modification date: 2021-08-04)

Primary citation

Pellegrino, S.,Demeshkina, N.,Mancera-Martinez, E.,Melnikov, S.,Simonetti, A.,Myasnikov, A.,Yusupov, M.,Yusupova, G.,Hashem, Y.
Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance.
J. Mol. Biol., 430:2677-2687, 2018

PubMed Abstract: 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.

PubMed: 29886014
DOI: 10.1016/j.jmb.2018.06.006

Experimental method

ELECTRON MICROSCOPY (3.9 Å)