NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.
Fiche publication
Date publication
mars 2020
Journal
European biophysics journal : EBJ
Auteurs
Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat, Dr YUSUPOVA Gulnara
Tous les auteurs :
Golubev A, Fatkhullin B, Gabdulkhakov A, Bikmullin A, Nurullina L, Garaeva N, Islamov D, Klochkova E, Klochkov V, Aganov A, Khusainov I, Validov S, Yusupova G, Yusupov M, Usachev K
Lien Pubmed
Résumé
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.
Mots clés
Drug target, EF-P, NMR, Protein structure, Ribosome, Staphylococcus aureus, X-ray
Référence
Eur. Biophys. J.. 2020 Mar 9;: