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

FEBS Lett. 2020 Nov;594(21):3551-3567. doi: 10.1002/1873-3468.13915. Epub 2020 Sep 10.


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 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 10 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.

Keywords: Staphylococcus aureus; antibiotic resistance; drug targets; methyltransferases; rRNA modifications; ribosome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cryoelectron Microscopy*
  • Ligands
  • Models, Molecular
  • RNA, Messenger / chemistry
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Ribosomal, 16S / chemistry
  • RNA, Ribosomal, 23S / chemistry
  • RNA, Transfer / chemistry
  • RNA, Transfer / genetics
  • RNA, Transfer / metabolism
  • Reproducibility of Results
  • Ribosomes / chemistry*
  • Ribosomes / metabolism
  • Ribosomes / ultrastructure*
  • Staphylococcus aureus / chemistry*
  • Staphylococcus aureus / ultrastructure*


  • Ligands
  • RNA, Messenger
  • RNA, Ribosomal, 16S
  • RNA, Ribosomal, 23S
  • RNA, Transfer