8FKU

Human nucleolar pre-60S ribosomal subunit (State C2)

This is a non-PDB format compatible entry.

Summary for 8FKU

• Entry DOI: 10.2210/pdb8fku/pdb
• EMDB information: 29109 29145 29146 29147 29148 29149 29150 29151 29257
• Descriptor: 60S ribosomal protein L12, 60S ribosomal protein L17, 60S ribosomal protein L18, ... (55 entities in total)
• Functional Keywords: pre-60s ribosomal subunit, assembly intermediate, ribosome, nucleoprotein complex
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 50
• Total formula weight: 3693846.11

Authors

Vanden Broeck, A.,Klinge, S. (deposition date: 2022-12-21, release date: 2023-07-12, Last modification date: 2023-07-19)

Primary citation

Vanden Broeck, A.,Klinge, S.
Principles of human pre-60 S biogenesis.
Science, 381:eadh3892-eadh3892, 2023

PubMed Abstract: During the early stages of human large ribosomal subunit (60) biogenesis, an ensemble of assembly factors establishes and fine-tunes the essential RNA functional centers of pre-60 particles by an unknown mechanism. Here, we report a series of cryo-electron microscopy structures of human nucleolar and nuclear pre-60 assembly intermediates at resolutions of 2.5 to 3.2 angstroms. These structures show how protein interaction hubs tether assembly factor complexes to nucleolar particles and how guanosine triphosphatases and adenosine triphosphatase couple irreversible nucleotide hydrolysis steps to the installation of functional centers. Nuclear stages highlight how a conserved RNA-processing complex, the rixosome, couples large-scale RNA conformational changes with pre-ribosomal RNA processing by the RNA degradation machinery. Our ensemble of human pre-60 particles provides a rich foundation with which to elucidate the molecular principles of ribosome formation.

PubMed: 37410842
DOI: 10.1126/science.adh3892

Experimental method

ELECTRON MICROSCOPY (2.82 Å)