5NJT
Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization.
This is a non-PDB format compatible entry.
Summary for 5NJT
| Entry DOI | 10.2210/pdb5njt/pdb |
| EMDB information | 3656 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (51 entities in total) |
| Functional Keywords | 100s, bacillus subtilis, cryo-em, hibernation, hpf, rmf, rrna, yvyd, translation |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 More |
| Total number of polymer chains | 51 |
| Total formula weight | 2111700.32 |
| Authors | Beckert, B.,Abdelshahid, M.,Schaefer, H.,Steinchen, W.,Arenz, S.,Berninghausen, O.,Beckmann, R.,Bange, G.,Turgay, K.,Wilson, D.N. (deposition date: 2017-03-29, release date: 2017-06-14, Last modification date: 2024-05-15) |
| Primary citation | Beckert, B.,Abdelshahid, M.,Schafer, H.,Steinchen, W.,Arenz, S.,Berninghausen, O.,Beckmann, R.,Bange, G.,Turgay, K.,Wilson, D.N. Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization. EMBO J., 36:2061-2072, 2017 Cited by PubMed Abstract: Under stress conditions, such as nutrient deprivation, bacteria enter into a hibernation stage, which is characterized by the appearance of 100S ribosomal particles. In , dimerization of 70S ribosomes into 100S requires the action of the ribosome modulation factor (RMF) and the hibernation-promoting factor (HPF). Most other bacteria lack RMF and instead contain a long form HPF (LHPF), which is necessary and sufficient for 100S formation. While some structural information exists as to how RMF and HPF mediate formation of 100S (100S), structural insight into 100S formation by LHPF has so far been lacking. Here we present a cryo-EM structure of the hibernating 100S (100S), revealing that the C-terminal domain (CTD) of the LHPF occupies a site on the 30S platform distinct from RMF Moreover, unlike RMF, the HPF-CTD is directly involved in forming the dimer interface, thereby illustrating the divergent mechanisms by which 100S formation is mediated in the majority of bacteria that contain LHPF, compared to some γ-proteobacteria, such as . PubMed: 28468753DOI: 10.15252/embj.201696189 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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