6T7O
X-ray structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)
Replaces: 5OOXSummary for 6T7O
| Entry DOI | 10.2210/pdb6t7o/pdb |
| Descriptor | Ribosome hibernation promotion factor (2 entities in total) |
| Functional Keywords | hpf, ribosome, staphylococcus aureus, hibernating promoting factor, ribosomal protein |
| Biological source | Staphylococcus aureus (strain NCTC 8325) |
| Total number of polymer chains | 2 |
| Total formula weight | 15905.90 |
| Authors | Fatkhullin, B.F.,Khusainov, I.S.,Ayupov, R.K.,Gabdulkhakov, A.G.,Tishchenko, S.V.,Validov, S.Z.,Yusupov, M.M. (deposition date: 2019-10-22, release date: 2019-12-11, Last modification date: 2024-01-24) |
| Primary citation | Usachev, K.S.,Fatkhullin, B.F.,Klochkova, E.A.,Miftakhov, A.K.,Golubev, A.A.,Bikmullin, A.G.,Nurullina, L.I.,Garaeva, N.S.,Islamov, D.R.,Gabdulkhakov, A.G.,Lekontseva, N.V.,Tishchenko, S.V.,Balobanov, V.A.,Khusainov, I.S.,Yusupov, M.M.,Validov, S.Z. Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization. J.Struct.Biol., 209:107408-107408, 2020 Cited by PubMed Abstract: Staphylococcus aureus hibernation promoting factor (SaHPF) is responsible for the formation of 100S ribosome dimers, which in turn help this pathogen to reduce energy spent under unfavorable conditions. Ribosome dimer formation strongly depends on the dimerization of the C-terminal domain of SaHPF (CTD). In this study, we solved the crystal structure of CTD at 1.6 Å resolution and obtained a precise arrangement of the dimer interface. Residues Phe, Val, Thr, Ile, Tyr, Ile andThr in the dimer interface of SaHPF protein were mutated and the effects were analyzed for the formation of 100S disomes of ribosomes isolated from S. aureus. It was shown that substitution of any of single residues Phe, Val, Ile, Tyr and Ile in the SaHPF homodimer interface abolished the ribosome dimerization in vitro. PubMed: 31669310DOI: 10.1016/j.jsb.2019.107408 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.60003624659 Å) |
Structure validation
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