Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8FKW

Human nucleolar pre-60S ribosomal subunit (State D2)

This is a non-PDB format compatible entry.
Summary for 8FKW
Entry DOI10.2210/pdb8fkw/pdb
EMDB information29111 29151 29156 29157 29158 29159 29160 29161 29162 29163 29164 29165 29259
Descriptor60S ribosomal protein L12, 60S ribosomal protein L17, 60S ribosomal protein L18, ... (58 entities in total)
Functional Keywordspre-60s ribosomal subunit, assembly intermediate, ribosome, nucleoprotein complex
Biological sourceHomo sapiens (human)
More
Total number of polymer chains53
Total formula weight3886103.66
Authors
Vanden Broeck, A.,Klinge, S. (deposition date: 2022-12-21, release date: 2023-07-12, Last modification date: 2023-08-16)
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 (2.5 Å)
Structure validation

226707

数据于2024-10-30公开中

PDB statisticsPDBj update infoContact PDBjnumon