NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus

Eur Biophys J. 2020 May;49(3-4):223-230. doi: 10.1007/s00249-020-01428-x. Epub 2020 Mar 9.


Elongation factor P (EF-P) is a translation protein factor that plays an important role in specialized translation of consecutive proline amino acid motifs. EF-P is an essential protein for cell fitness in native environmental conditions. It regulates synthesis of proteins involved in bacterial motility, environmental adaptation and bacterial virulence, thus making EF-P a potential drug target. In the present study, we determined the solution and crystal structure of EF-P from the pathogenic bacteria Staphylococcus aureus at 1.48 Å resolution. The structure can serve as a platform for structure-based drug design of novel antibiotics to combat the growing antibiotic resistance of S. aureus.

Keywords: Drug target; EF-P; NMR; Protein structure; Ribosome; Staphylococcus aureus; X-ray.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallography, X-Ray
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular*
  • Peptide Elongation Factors / chemistry*
  • Peptide Elongation Factors / metabolism
  • Protein Domains
  • Staphylococcus aureus*


  • Bacterial Proteins
  • Peptide Elongation Factors
  • factor EF-P