9SDA
Cryo-EM structure of the 70S ribosome from Francisella tularensis bound to a hibernation-promoting factor
This is a non-PDB format compatible entry.
Summary for 9SDA
| Entry DOI | 10.2210/pdb9sda/pdb |
| EMDB information | 54782 |
| Descriptor | Chains: A, Large ribosomal subunit protein uL14, Large ribosomal subunit protein uL15, ... (55 entities in total) |
| Functional Keywords | cryo-em structure of the 70s ribosome from francisella tularensis bound to a hibernation-promoting factor from hpf/yfia family, ribosome |
| Biological source | Francisella tularensis More |
| Total number of polymer chains | 53 |
| Total formula weight | 2137673.64 |
| Authors | |
| Primary citation | Klima, M.,Silhan, J.,Pavlik, P.,Hercik, K.,Boura, E. Structure of the hibernating Francisella tularensis ribosome and mechanistic insights into its inhibition by antibiotics. Nucleic Acids Res., 54:-, 2026 Cited by PubMed Abstract: Francisella tularensis is the causative agent of tularemia, a zoonotic disease named after the Tulare County, California. Symptoms include sudden fever, chills, fatigue, and swollen lymph nodes, among others, and without treatment it is very serious or even fatal. In addition, F. tularensis is considered a potential bioterrorism threat due to its high infectivity and lethality. Ribosomes are key targets for many classes of antibiotics. In this study, we examined the F. tularensis ribosome and determined its structure at 2.5Å resolution using cryo-electron microscopy. Notably, we observed the stress-induced ribosome-associated inhibitor A (RaiA) protein bound to the ribosome. RaiA functions as a molecular hibernation factor, inhibiting bacterial translation in response to stress or nutrient deprivation. This mechanism parallels that described in the model organism Escherichia coli and in several pathogenic bacteria, such as Staphylococcus aureus. Furthermore, we solved structures of the antibiotics chloramphenicol and gentamicin bound to the F. tularensis ribosome. Collectively, these results provide structural insights that highlight previously unexplored opportunities for therapeutic intervention. PubMed: 42049235DOI: 10.1093/nar/gkag340 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.39 Å) |
Structure validation
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