9SDA
Cryo-EM structure of the 70S ribosome from Francisella tularensis bound to a hibernation-promoting factor
これはPDB形式変換不可エントリーです。
9SDA の概要
| エントリーDOI | 10.2210/pdb9sda/pdb |
| EMDBエントリー | 54782 |
| 分子名称 | Chains: A, Large ribosomal subunit protein uL14, Large ribosomal subunit protein uL15, ... (55 entities in total) |
| 機能のキーワード | cryo-em structure of the 70s ribosome from francisella tularensis bound to a hibernation-promoting factor from hpf/yfia family, ribosome |
| 由来する生物種 | Francisella tularensis 詳細 |
| タンパク質・核酸の鎖数 | 53 |
| 化学式量合計 | 2137673.64 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.39 Å) |
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