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8FKP

Human nucleolar pre-60S ribosomal subunit (State A1)

This is a non-PDB format compatible entry.
Summary for 8FKP
Entry DOI10.2210/pdb8fkp/pdb
EMDB information29104 29128 29129 29130 29131 29134 29135 29151 29252 29253 29254 29255 29256 29257 29258 29259 29260 29261 29262 29263 29265 29266 29267 29268 29269 29271 29272 29273 29274 29275 29276 29277
Descriptor5.8S rRNA, 60S ribosomal protein L18a, 60S ribosomal protein L21, ... (50 entities in total)
Functional Keywordspre-60s ribosomal subunit, assembly intermediate, ribosome, nucleoprotein complex
Biological sourceHomo sapiens (human)
More
Total number of polymer chains47
Total formula weight3628542.16
Authors
Vanden Broeck, A.,Klinge, S. (deposition date: 2022-12-21, release date: 2023-07-12, Last modification date: 2024-05-01)
Primary citationVanden Broeck, A.,Klinge, S.
Principles of human pre-60 S biogenesis.
Science, 381:eadh3892-eadh3892, 2023
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.85 Å)
Structure validation

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