SNAP annotations: PDB entry 6gqv

PDB-id

6gqv; DSSR-derived features in text and JSON formats; DNAproDB

Class

ribosome

Method

cryo-EM (4.0 Å)

Summary

cryo-EM recosntruction of yeast 80s ribosome in complex with mrna, trna and eef2 (gmppcp)

Reference

Pellegrino S, Demeshkina N, Mancera-Martinez E, Melnikov S, Simonetti A, Myasnikov A, Yusupov M, Yusupova G, Hashem Y (2018): "Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance." J. Mol. Biol., 430, 2677-2687. doi: 10.1016/j.jmb.2018.06.006.

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.