Summary for 4V8H
| Entry DOI | 10.2210/pdb4v8h/pdb |
| Descriptor | 16S Ribosomal RNA, 30S Ribosomal Protein S10, 30S Ribosomal Protein S11, ... (56 entities in total) |
| Functional Keywords | ribosome hibernation factor, yhbh, protein e, stress response, stationary phase, ribosome hibernation, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 106 |
| Total formula weight | 4400353.83 |
| Authors | Polikanov, Y.S.,Blaha, G.M.,Steitz, T.A. (deposition date: 2011-12-11, release date: 2014-07-09, Last modification date: 2023-09-20) |
| Primary citation | Polikanov, Y.S.,Blaha, G.M.,Steitz, T.A. How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis. Science, 336:915-918, 2012 Cited by PubMed Abstract: Eubacteria inactivate their ribosomes as 100S dimers or 70S monomers upon entry into stationary phase. In Escherichia coli, 100S dimer formation is mediated by ribosome modulation factor (RMF) and hibernation promoting factor (HPF), or alternatively, the YfiA protein inactivates ribosomes as 70S monomers. Here, we present high-resolution crystal structures of the Thermus thermophilus 70S ribosome in complex with each of these stationary-phase factors. The binding site of RMF overlaps with that of the messenger RNA (mRNA) Shine-Dalgarno sequence, which prevents the interaction between the mRNA and the 16S ribosomal RNA. The nearly identical binding sites of HPF and YfiA overlap with those of the mRNA, transfer RNA, and initiation factors, which prevents translation initiation. The binding of RMF and HPF, but not YfiA, to the ribosome induces a conformational change of the 30S head domain that promotes 100S dimer formation. PubMed: 22605777DOI: 10.1126/science.1218538 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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