Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 A resolution.

ABSTRACT: Single-particle cryogenic electron microscopy (cryo-EM) has become a standard technique for determining protein structures at atomic resolution^1-3. 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 relationships⁴, 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 p

SUBMITTER: Su Z 

PROVIDER: S-EPMC8405103 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature