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

https://www.ncbi.nlm.nih.gov/pubmed/31165320

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.