8BXA
Crystal structure of ribosome binding factor A (RbfA) from S. aureus
8BXA の概要
エントリーDOI | 10.2210/pdb8bxa/pdb |
分子名称 | Ribosome-binding factor A (2 entities in total) |
機能のキーワード | ribosome, maturation, 30s subunit, s. aureus |
由来する生物種 | Staphylococcus aureus subsp. aureus NCTC 8325 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 13535.72 |
構造登録者 | Fatkhullin, B.,Bikmullin, A.,Gabdulkhakov, A.,Khusainov, I.,Validov, S.,Usachev, K.,Yusupov, M. (登録日: 2022-12-08, 公開日: 2023-02-22, 最終更新日: 2024-06-19) |
主引用文献 | Bikmullin, A.G.,Fatkhullin, B.,Stetsenko, A.,Gabdulkhakov, A.,Garaeva, N.,Nurullina, L.,Klochkova, E.,Golubev, A.,Khusainov, I.,Trachtmann, N.,Blokhin, D.,Guskov, A.,Validov, S.,Usachev, K.,Yusupov, M. Yet Another Similarity between Mitochondrial and Bacterial Ribosomal Small Subunit Biogenesis Obtained by Structural Characterization of RbfA from S. aureus. Int J Mol Sci, 24:-, 2023 Cited by PubMed Abstract: Ribosome biogenesis is a complex and highly accurate conservative process of ribosomal subunit maturation followed by association. Subunit maturation comprises sequential stages of ribosomal RNA and proteins' folding, modification and binding, with the involvement of numerous RNAses, helicases, GTPases, chaperones, RNA, protein-modifying enzymes, and assembly factors. One such assembly factor involved in bacterial 30S subunit maturation is ribosomal binding factor A (RbfA). In this study, we present the crystal (determined at 2.2 Å resolution) and NMR structures of RbfA as well as the 2.9 Å resolution cryo-EM reconstruction of the 30S-RbfA complex from (). Additionally, we show that the manner of RbfA action on the small ribosomal subunit during its maturation is shared between bacteria and mitochondria. The obtained results clarify the function of RbfA in the 30S maturation process and its role in ribosome functioning in general. Furthermore, given that is a serious human pathogen, this study provides an additional prospect to develop antimicrobials targeting bacterial pathogens. PubMed: 36768442DOI: 10.3390/ijms24032118 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.22 Å) |
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