Structural highlights
Function
RLA0_YEAST Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Publication Abstract from PubMed
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.
Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance.,Pellegrino S, Demeshkina N, Mancera-Martinez E, Melnikov S, Simonetti A, Myasnikov A, Yusupov M, Yusupova G, Hashem Y J Mol Biol. 2018 Jun 7. pii: S0022-2836(18)30582-5. doi:, 10.1016/j.jmb.2018.06.006. PMID:29886014[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 2018 Jun 7. pii: S0022-2836(18)30582-5. doi:, 10.1016/j.jmb.2018.06.006. PMID:29886014 doi:http://dx.doi.org/10.1016/j.jmb.2018.06.006
