EMD-0373

Single-particle
3.8 Å
EMD-0373 Deposition: 29/11/2018
Map released: 13/03/2019
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-0373

Cryo-EM structure of Lsg1-engaged (LE) pre-60S ribosomal subunit

EMD-0373

Single-particle
3.8 Å
EMD-0373 Deposition: 29/11/2018
Map released: 13/03/2019
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sample: Lsg1-engaged (LE) pre-60S ribosomal subunit
Fitted models: 6n8n (Avg. Q-score: 0.457)

Deposition Authors: Zhou Y , Musalgaonkar S
Tightly-orchestrated rearrangements govern catalytic center assembly of the ribosome.
Zhou Y , Musalgaonkar S, Johnson AW , Taylor DW
(2019) Nat Commun , 10 , 958 - 958
PUBMED: 30814529
DOI: doi:10.1038/s41467-019-08880-0
ISSN: 2041-1723
Abstract:
The catalytic activity of the ribosome is mediated by RNA, yet proteins are essential for the function of the peptidyl transferase center (PTC). In eukaryotes, final assembly of the PTC occurs in the cytoplasm by insertion of the ribosomal protein Rpl10 (uL16). We determine structures of six intermediates in late nuclear and cytoplasmic maturation of the large subunit that reveal a tightly-choreographed sequence of protein and RNA rearrangements controlling the insertion of Rpl10. We also determine the structure of the biogenesis factor Yvh1 and show how it promotes assembly of the P stalk, a critical element for recruitment of GTPases that drive translation. Together, our structures provide a blueprint for final assembly of a functional ribosome.