6GQV
Cryo-EM recosntruction of yeast 80S ribosome in complex with mRNA, tRNA and eEF2 (GMPPCP)
This is a non-PDB format compatible entry.
Summary for 6GQV
| Entry DOI | 10.2210/pdb6gqv/pdb |
| Related | 6GQ1 6GQB |
| EMDB information | 0047 0048 0049 |
| Descriptor | 25S ribosomal RNA, 60S ribosomal protein L6-A, 60S ribosomal protein L7-A, ... (86 entities in total) |
| Functional Keywords | eukaryotic 80s ribosome, diphthamide, eef2, translation fidelity, mrna-trna translocation, ribosome |
| Biological source | Saccharomyces cerevisiae More |
| Total number of polymer chains | 84 |
| Total formula weight | 3191429.53 |
| Authors | Pellegrino, S.,Yusupov, M.,Yusupova, G.,Hashem, Y. (deposition date: 2018-06-08, release date: 2018-07-11, Last modification date: 2018-08-08) |
| 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 Cited by 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: 29886014DOI: 10.1016/j.jmb.2018.06.006 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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