8BYV
Cryo-EM structure of a Staphylococus aureus 30S-RbfA complex
Summary for 8BYV
| Entry DOI | 10.2210/pdb8byv/pdb |
| Related | 8BXA |
| EMDB information | 16334 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (21 entities in total) |
| Functional Keywords | ribosome, rbfa, 30s subunit maturation, cryo-em, ribosome biogenesis, translation, staphylococcus aureus |
| Biological source | Staphylococcus aureus subsp. aureus NCTC 8325 More |
| Total number of polymer chains | 21 |
| Total formula weight | 789244.25 |
| Authors | Bikmullin, A.G.,Fatkhullin, B.,Stetsenko, A.,Guskov, A.,Yusupov, M. (deposition date: 2022-12-14, release date: 2023-12-27, Last modification date: 2024-07-10) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.89 Å) |
Structure validation
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