8P5D

Spraguea lophii ribosome in the closed conformation by cryo sub tomogram averaging

This is a non-PDB format compatible entry.

Replaces:  8BR3

Summary for 8P5D

• Entry DOI: 10.2210/pdb8p5d/pdb
• Related: 7QCA 7QJH
• EMDB information: 16198 17448
• Descriptor: RNA 28S, 60S ribosomal protein L6, 60S ribosomal protein L32, ... (76 entities in total)
• Functional Keywords: microsporidia, ribosome
• Biological source: Spraguea lophii 42_110; More
• Total number of polymer chains: 75
• Total formula weight: 2647098.70

Authors

Gil Diez, P.,McLaren, M.,Isupov, M.N.,Daum, B.,Conners, R.,Williams, B. (deposition date: 2023-05-23, release date: 2023-06-21, Last modification date: 2023-12-20)

Primary citation

McLaren, M.,Conners, R.,Isupov, M.N.,Gil-Diez, P.,Gambelli, L.,Gold, V.A.M.,Walter, A.,Connell, S.R.,Williams, B.,Daum, B.
CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state.
Nat Microbiol, 8:1834-1845, 2023

PubMed Abstract: Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be shut down almost entirely by inhibiting ribosomal function. Here we investigated eukaryotic hibernating ribosomes from the microsporidian parasite Spraguea lophii in situ by a combination of electron cryo-tomography and single-particle electron cryo-microscopy. We show that microsporidian spores contain hibernating ribosomes that are locked in a dimeric (100S) state, which is formed by a unique dimerization mechanism involving the beak region. The ribosomes within the dimer are fully assembled, suggesting that they are ready to be activated once the host cell is invaded. This study provides structural evidence for dimerization acting as a mechanism for ribosomal hibernation in microsporidia, and therefore demonstrates that eukaryotes utilize this mechanism in translational control.

PubMed: 37709902
DOI: 10.1038/s41564-023-01469-w

Experimental method

ELECTRON MICROSCOPY (10.8 Å)