Cryo‐EM structure of the ribosome functional complex of the human pathogen Staphylococcus aureus at 3.2 Å resolution

Alexander Golubev (1, 2) , Bulat Fatkhullin (1, 3) , Iskander Khusainov (1, 4) , Lasse Jenner (2) , Azat Gabdulkhakov (1, 3) , Shamil Validov (1) , Marat Yusupov (1, 2) , Gulnara Yusupova (2) , Konstantin Usachev (1)

1 KFU - Kazan Federal University
2 IGBMC - Institut de Génétique et de Biologie Moléculaire et Cellulaire
3 Institute of Protein Research
4 MPIBP - Max-Planck-Institut für Biophysik - Max Planck Institute of Biophysics

Staphylococcus aureus is a bacterial pathogen and one of the leading causes of healthcare-acquired infections in the world. The growing antibiotic resistance of S. aureus obliges us to search for new drugs Accepted Article This article is protected by copyright. All rights reserved and treatments. As the majority of antibiotics target the ribosome, knowledge of its detailed structure is crucial for drug development. Here, we report the Cryo-EM reconstruction at 3.2 Å resolution of the S. aureus ribosome with P-site tRNA, messenger RNA and ten RNA modification sites previously not assigned or visualized. The resulting model is the most precise and complete high-resolution structure to date of the S. aureus 70S ribosome with functional ligands.

Mots clés: Ribosome; rRNA modifications; Staphylococcus aureus; methyltransferases; antibiotic resistance; drug targets; Ribosome

Domaines: Bactériologie; Biologie structurale [q-bio.BM]

Alexander Golubev, Bulat Fatkhullin, Iskander Khusainov, Lasse Jenner, Azat Gabdulkhakov, et al.. Cryo‐EM structure of the ribosome functional complex of the human pathogen Staphylococcus aureus at 3.2 Å resolution. FEBS Letters, 2020, 594 (21), pp.3551 - 3567. ⟨10.1002/1873-3468.13915⟩. ⟨hal-03373743⟩