| Autor: |
Konstantin S, Usachev, Shamil Z, Validov, Iskander Sh, Khusainov, Alexander A, Varfolomeev, Vladimir V, Klochkov, Albert V, Aganov, Marat M, Yusupov |
| Rok vydání: |
2019 |
| Předmět: |
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| Zdroj: |
Journal of biomolecular NMR. 73(5) |
| ISSN: |
1573-5001 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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