7EZ2
Holo L-16 ScaI Tetrahymena ribozyme
7EZ2 の概要
エントリーDOI | 10.2210/pdb7ez2/pdb |
EMDBエントリー | 31385 31386 |
分子名称 | Holo L-16 ScaI Tetrahymena ribozyme S1, Holo L-16 ScaI Tetrahymena ribozyme S2, Holo L-16 ScaI Tetrahymena ribozyme, ... (4 entities in total) |
機能のキーワード | rna structure, tetrahymena ribozyme, rna |
由来する生物種 | Tetrahymena thermophila 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 131749.87 |
構造登録者 | |
主引用文献 | Su, Z.,Zhang, K.,Kappel, K.,Li, S.,Palo, M.Z.,Pintilie, G.D.,Rangan, R.,Luo, B.,Wei, Y.,Das, R.,Chiu, W. Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 angstrom resolution. Nature, 596:603-607, 2021 Cited by PubMed Abstract: Single-particle cryogenic electron microscopy (cryo-EM) has become a standard technique for determining protein structures at atomic resolution. However, cryo-EM studies of protein-free RNA are in their early days. The Tetrahymena thermophila group I self-splicing intron was the first ribozyme to be discovered and has been a prominent model system for the study of RNA catalysis and structure-function relationships, but its full structure remains unknown. Here we report cryo-EM structures of the full-length Tetrahymena ribozyme in substrate-free and bound states at a resolution of 3.1 Å. Newly resolved peripheral regions form two coaxially stacked helices; these are interconnected by two kissing loop pseudoknots that wrap around the catalytic core and include two previously unforeseen (to our knowledge) tertiary interactions. The global architecture is nearly identical in both states; only the internal guide sequence and guanosine binding site undergo a large conformational change and a localized shift, respectively, upon binding of RNA substrates. These results provide a long-sought structural view of a paradigmatic RNA enzyme and signal a new era for the cryo-EM-based study of structure-function relationships in ribozymes. PubMed: 34381213DOI: 10.1038/s41586-021-03803-w 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.05 Å) |
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