6QBZ

Solution structure of the N-terminal domain of the Staphylococcus aureus Hibernation Promoting Factor

Summary for 6QBZ

• Entry DOI: 10.2210/pdb6qbz/pdb
• NMR Information: BMRB: 27085
• Descriptor: Ribosome hibernation promoting factor (1 entity in total)
• Functional Keywords: hibernation promoting factor, staphylococcus aureus, 100s ribosome, ribosomal protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 12930.72

Authors

Usachev, K.S.,Validov, S.Z.,Khusainov, I.S.,Klochkov, V.V.,Aganov, A.V.,Yusupov, M.M. (deposition date: 2018-12-25, release date: 2019-06-19, Last modification date: 2024-05-15)

Primary citation

Usachev, K.S.,Validov, S.Z.,Khusainov, I.S.,Varfolomeev, A.A.,Klochkov, V.V.,Aganov, A.V.,Yusupov, M.M.
Solution structure of the N-terminal domain of the Staphylococcus aureus hibernation promoting factor.
J.Biomol.Nmr, 73:223-227, 2019

PubMed Abstract: 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.

PubMed: 31165320
DOI: 10.1007/s10858-019-00254-4

Experimental method

SOLUTION NMR