Structural highlights
Function
[W8USK0_STAAU] Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth.[HAMAP-Rule:MF_00839]
Publication Abstract from PubMed
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.
Solution structure of the N-terminal domain of the Staphylococcus aureus hibernation promoting factor.,Usachev KS, Validov SZ, Khusainov IS, Varfolomeev AA, Klochkov VV, Aganov AV, Yusupov MM J Biomol NMR. 2019 May;73(5):223-227. doi: 10.1007/s10858-019-00254-4. Epub 2019 , Jun 4. PMID:31165320[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Usachev KS, Validov SZ, Khusainov IS, Varfolomeev AA, Klochkov VV, Aganov AV, Yusupov MM. Solution structure of the N-terminal domain of the Staphylococcus aureus hibernation promoting factor. J Biomol NMR. 2019 May;73(5):223-227. doi: 10.1007/s10858-019-00254-4. Epub 2019 , Jun 4. PMID:31165320 doi:http://dx.doi.org/10.1007/s10858-019-00254-4
