9FO0

PF30S ribosomal subunit - control

This is a non-PDB format compatible entry.

Summary for 9FO0

• Entry DOI: 10.2210/pdb9fo0/pdb
• EMDB information: 50613
• Descriptor: RNA-binding protein, Small ribosomal subunit protein uS5, Small ribosomal subunit protein eS6, ... (29 entities in total)
• Functional Keywords: pyrococcus furiosus, ribosomal subunit, dimerization, anti-association, ribosome-associated protein, translation
• Biological source: Pyrococcus furiosus; More
• Total number of polymer chains: 29
• Total formula weight: 911161.77

Authors

Hassan, A.H.,Demo, G. (deposition date: 2024-06-11, release date: 2025-01-15, Last modification date: 2025-01-22)

Primary citation

Hassan, A.H.,Pinkas, M.,Yaeshima, C.,Ishino, S.,Uchiumi, T.,Ito, K.,Demo, G.
Novel archaeal ribosome dimerization factor facilitating unique 30S-30S dimerization.
Nucleic Acids Res., 53:-, 2025

PubMed Abstract: Protein synthesis (translation) consumes a substantial proportion of cellular resources, prompting specialized mechanisms to reduce translation under adverse conditions. Ribosome inactivation often involves ribosome-interacting proteins. In both bacteria and eukaryotes, various ribosome-interacting proteins facilitate ribosome dimerization or hibernation, and/or prevent ribosomal subunits from associating, enabling the organisms to adapt to stress. Despite extensive studies on bacteria and eukaryotes, understanding factor-mediated ribosome dimerization or anti-association in archaea remains elusive. Here, we present cryo-electron microscopy structures of an archaeal 30S dimer complexed with an archaeal ribosome dimerization factor (designated aRDF), from Pyrococcus furiosus, resolved at a resolution of 3.2 Å. The complex features two 30S subunits stabilized by aRDF homodimers in a unique head-to-body architecture, which differs from the disome architecture observed during hibernation in bacteria and eukaryotes. aRDF interacts directly with eS32 ribosomal protein, which is essential for subunit association. The binding mode of aRDF elucidates its anti-association properties, which prevent the assembly of archaeal 70S ribosomes.

PubMed: 39797736
DOI: 10.1093/nar/gkae1324

Experimental method

ELECTRON MICROSCOPY (3.4 Å)