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-Structure paper
タイトル | Molecular basis of tRNA recognition by the Elongator complex. |
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ジャーナル・号・ページ | Sci Adv, Vol. 5, Issue 7, Page eaaw2326, Year 2019 |
掲載日 | 2019年7月10日 |
著者 | Maria I Dauden / Marcin Jaciuk / Felix Weis / Ting-Yu Lin / Carolin Kleindienst / Nour El Hana Abbassi / Heena Khatter / Rościsław Krutyhołowa / Karin D Breunig / Jan Kosinski / Christoph W Müller / Sebastian Glatt / |
PubMed 要旨 | The highly conserved Elongator complex modifies transfer RNAs (tRNAs) in their wobble base position, thereby regulating protein synthesis and ensuring proteome stability. The precise mechanisms of ...The highly conserved Elongator complex modifies transfer RNAs (tRNAs) in their wobble base position, thereby regulating protein synthesis and ensuring proteome stability. The precise mechanisms of tRNA recognition and its modification reaction remain elusive. Here, we show cryo-electron microscopy structures of the catalytic subcomplex of Elongator and its tRNA-bound state at resolutions of 3.3 and 4.4 Å. The structures resolve details of the catalytic site, including the substrate tRNA, the iron-sulfur cluster, and a SAM molecule, which are all validated by mutational analyses in vitro and in vivo. tRNA binding induces conformational rearrangements, which precisely position the targeted anticodon base in the active site. Our results provide the molecular basis for substrate recognition of Elongator, essential to understand its cellular function and role in neurodegenerative diseases and cancer. |
リンク | Sci Adv / PubMed:31309145 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 - 6.7 Å |
構造データ | EMDB-4573: EMDB-4574: EMDB-4576: |
化合物 | ChemComp-SF4: ChemComp-5AD: |
由来 |
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キーワード | TRANSLATION / Elongator / yeast / tRNA modification / Elp123 |