4V8H の概要
エントリーDOI | 10.2210/pdb4v8h/pdb |
分子名称 | 16S Ribosomal RNA, 30S Ribosomal Protein S10, 30S Ribosomal Protein S11, ... (56 entities in total) |
機能のキーワード | ribosome hibernation factor, yhbh, protein e, stress response, stationary phase, ribosome hibernation, ribosome |
由来する生物種 | Escherichia coli 詳細 |
タンパク質・核酸の鎖数 | 106 |
化学式量合計 | 4400353.83 |
構造登録者 | |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.1 Å) |
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