EMD-4215

Single-particle
3.1 Å
EMD-4215 Deposition: 15/12/2017
Map released: 28/02/2018
Last modified: 11/04/2018
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-4215

Yeast 80S ribosome with an uncleaved 20S rRNA

EMD-4215

Single-particle
3.1 Å
EMD-4215 Deposition: 15/12/2017
Map released: 28/02/2018
Last modified: 11/04/2018
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae
Sample: Cytoplasmic yeast 80S ribosome with a uncleaved 20S rRNA

Deposition Authors: Scaiola A, Pena C, Weisser M, Boehringer D, Leibundgut M, Klingauf-Nerurkar P, Gerhardy S, Panse VG, Ban N
Structure of a eukaryotic cytoplasmic pre-40S ribosomal subunit.
PUBMED: 29459436
DOI: doi:10.15252/embj.201798499
ISSN: 1460-2075
ASTM: EMJODG
Abstract:
Final maturation of eukaryotic ribosomes occurs in the cytoplasm and requires the sequential removal of associated assembly factors and processing of the immature 20S pre-RNA Using cryo-electron microscopy (cryo-EM), we have determined the structure of a yeast cytoplasmic pre-40S particle in complex with Enp1, Ltv1, Rio2, Tsr1, and Pno1 assembly factors poised to initiate final maturation. The structure reveals that the pre-rRNA adopts a highly distorted conformation of its 3' major and 3' minor domains stabilized by the binding of the assembly factors. This observation is consistent with a mechanism that involves concerted release of the assembly factors orchestrated by the folding of the rRNA in the head of the pre-40S subunit during the final stages of maturation. Our results provide a structural framework for the coordination of the final maturation events that drive a pre-40S particle toward the mature form capable of engaging in translation.