8V9J
Cryo-EM structure of the Mycobacterium smegmatis 70S ribosome in complex with hibernation factor Msmeg1130 (Balon) (Structure 4)
This is a non-PDB format compatible entry.
Summary for 8V9J
| Entry DOI | 10.2210/pdb8v9j/pdb |
| EMDB information | 43074 |
| Descriptor | 16S Ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (60 entities in total) |
| Functional Keywords | cryo-em, mycobacteria, hibernation, msmeg1130, balon, ribosome |
| Biological source | Mycolicibacterium smegmatis MC2 155 More |
| Total number of polymer chains | 59 |
| Total formula weight | 2386159.43 |
| Authors | Rybak, M.Y.,Helena-Bueno, K.,Hill, C.H.,Melnikov, S.V.,Gagnon, M.G. (deposition date: 2023-12-08, release date: 2024-02-07, Last modification date: 2024-03-13) |
| Primary citation | Helena-Bueno, K.,Rybak, M.Y.,Ekemezie, C.L.,Sullivan, R.,Brown, C.R.,Dingwall, C.,Basle, A.,Schneider, C.,Connolly, J.P.R.,Blaza, J.N.,Csorgo, B.,Moynihan, P.J.,Gagnon, M.G.,Hill, C.H.,Melnikov, S.V. A new family of bacterial ribosome hibernation factors. Nature, 626:1125-1132, 2024 Cited by PubMed Abstract: To conserve energy during starvation and stress, many organisms use hibernation factor proteins to inhibit protein synthesis and protect their ribosomes from damage. In bacteria, two families of hibernation factors have been described, but the low conservation of these proteins and the huge diversity of species, habitats and environmental stressors have confounded their discovery. Here, by combining cryogenic electron microscopy, genetics and biochemistry, we identify Balon, a new hibernation factor in the cold-adapted bacterium Psychrobacter urativorans. We show that Balon is a distant homologue of the archaeo-eukaryotic translation factor aeRF1 and is found in 20% of representative bacteria. During cold shock or stationary phase, Balon occupies the ribosomal A site in both vacant and actively translating ribosomes in complex with EF-Tu, highlighting an unexpected role for EF-Tu in the cellular stress response. Unlike typical A-site substrates, Balon binds to ribosomes in an mRNA-independent manner, initiating a new mode of ribosome hibernation that can commence while ribosomes are still engaged in protein synthesis. Our work suggests that Balon-EF-Tu-regulated ribosome hibernation is a ubiquitous bacterial stress-response mechanism, and we demonstrate that putative Balon homologues in Mycobacteria bind to ribosomes in a similar fashion. This finding calls for a revision of the current model of ribosome hibernation inferred from common model organisms and holds numerous implications for how we understand and study ribosome hibernation. PubMed: 38355796DOI: 10.1038/s41586-024-07041-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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