7EZ2
Holo L-16 ScaI Tetrahymena ribozyme
Summary for 7EZ2
| Entry DOI | 10.2210/pdb7ez2/pdb |
| EMDB information | 31385 31386 |
| Descriptor | Holo L-16 ScaI Tetrahymena ribozyme S1, Holo L-16 ScaI Tetrahymena ribozyme S2, Holo L-16 ScaI Tetrahymena ribozyme, ... (4 entities in total) |
| Functional Keywords | rna structure, tetrahymena ribozyme, rna |
| Biological source | Tetrahymena thermophila More |
| Total number of polymer chains | 3 |
| Total formula weight | 131749.87 |
| Authors | |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.05 Å) |
Structure validation
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