8BXA

Crystal structure of ribosome binding factor A (RbfA) from S. aureus

Summary for 8BXA

• Entry DOI: 10.2210/pdb8bxa/pdb
• Descriptor: Ribosome-binding factor A (2 entities in total)
• Functional Keywords: ribosome, maturation, 30s subunit, s. aureus
• Biological source: Staphylococcus aureus subsp. aureus NCTC 8325
• Total number of polymer chains: 1
• Total formula weight: 13535.72

Authors

Fatkhullin, B.,Bikmullin, A.,Gabdulkhakov, A.,Khusainov, I.,Validov, S.,Usachev, K.,Yusupov, M. (deposition date: 2022-12-08, release date: 2023-02-22, Last modification date: 2024-06-19)

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

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: 36768442
DOI: 10.3390/ijms24032118

Experimental method

X-RAY DIFFRACTION (2.22 Å)