Crystal structure of the GDP-bound GTPase Era from Staphylococcus aureus.
Fiche publication
Date publication
octobre 2024
Journal
Biochemical and biophysical research communications
Auteurs
Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat
Tous les auteurs :
Klochkova E, Biktimirov A, Islamov D, Belousov A, Validov S, Yusupov M, Usachev K
Lien Pubmed
Résumé
GTPase Era from Staphylococcus aureus belongs to the TRAFAC superfamily of the TrmE-Era-EngA-EngB-Septin-like GTPases class and plays a significant role in the vital activity of this pathogenic microorganism as a maturation factor of the 30S ribosome subunit. However, the functions of this protein are not fully understood, making it a promising object for further study. Here, the 2.76 Å resolution crystal structure of Staphylococcus aureus Era in complex with GDP is presented. Structural comparison with other GTP-bound and GDP-bound homologous proteins, GTPase domain and the KH domain revealed a mutual orientation in S. aureus which has not been described before. The GDP-bound Era structure presented here will facilitate efforts to elucidate its interactions with its regulators and lay the foundation for a structure-based search for specific inhibitors.
Mots clés
30S biogenesis, Bacterial ribosomal maturation factor, Era, GTPase, Ribosome, Staphylococcus aureus, Translation
Référence
Biochem Biophys Res Commun. 2024 10 18;735:150852