9FO09FO0 の概要
| エントリーDOI | 10.2210/pdb9fo0/pdb |
| EMDBエントリー | 50613 |
| 分子名称 | RNA-binding protein, Small ribosomal subunit protein uS5, Small ribosomal subunit protein eS6, ... (29 entities in total) |
| 機能のキーワード | pyrococcus furiosus, ribosomal subunit, dimerization, anti-association, ribosome-associated protein, translation |
| 由来する生物種 | Pyrococcus furiosus 詳細 |
| タンパク質・核酸の鎖数 | 29 |
| 化学式量合計 | 911161.77 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 39797736DOI: 10.1093/nar/gkae1324 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.4 Å) |
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