Solution structure of the N-terminal domain of the Staphylococcus aureus hibernation promoting factor.
Fiche publication
Date publication
mai 2019
Journal
Journal of biomolecular NMR
Auteurs
Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat
Tous les auteurs :
Usachev KS, Validov SZ, Khusainov IS, Varfolomeev AA, Klochkov VV, Aganov AV, Yusupov MM
Lien Pubmed
Résumé
Staphylococcus aureus hibernation promoting factor (SaHPF) is a 22,2 kDa protein which plays a crucial role in 100S Staphylococcus aureus ribosome formation during stress. SaHPF consists of N-terminal domain (NTD) that prevents proteins synthesis by binding to the 30S subunit at the P- and A-sites, connected through a flexible linker with a C-terminal domain (CTD) that keeps ribosomes in 100S form via homodimerization. Recently obtained 100S ribosome structure of S. aureus by cryo-EM shown that SaHPF-NTD bound to the ribosome active sites, however due to the absence of SaHPF-NTD structure it was modeled by homology with the E. coli hibernation factors HPF and YfiA. In present paper we have determined the solution structure of SaHPF-NTD by high-resolution NMR spectroscopy which allows us to increase structural knowledge about HPF structure from S. aureus.
Mots clés
100S ribosome, HPF, Hibernation promoting factor, Protein NMR, Staphylococcus aureus, Structure
Référence
J. Biomol. NMR. 2019 May;73(5):223-227