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-Structure paper
タイトル | Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance. |
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ジャーナル・号・ページ | J Mol Biol, Vol. 430, Issue 17, Page 2677-2687, Year 2018 |
掲載日 | 2018年8月17日 |
著者 | Simone Pellegrino / Natalia Demeshkina / Eder Mancera-Martinez / Sergey Melnikov / Angelita Simonetti / Alexander Myasnikov / Marat Yusupov / Gulnara Yusupova / Yaser Hashem / |
PubMed 要旨 | 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 ...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. |
リンク | J Mol Biol / PubMed:29886014 |
手法 | EM (単粒子) |
解像度 | 3.9 - 4.4 Å |
構造データ | EMDB-0047, PDB-6gq1: EMDB-0048, PDB-6gqb: EMDB-0049, PDB-6gqv: EMDB-0055: |
化合物 | ChemComp-ZN: ChemComp-SO1: ChemComp-GCP: ChemComp-GDP: ChemComp-ALF: |
由来 |
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キーワード | RIBOSOME / Eukaryotic 80S riboosme / mRNA-tRNA translocation / diphthamide / Eukaryotic 80S ribosome / eEF2 / translation fidelity |