2MF1
Structural basis of the non-coding RNA RsmZ acting as protein sponge: Conformer R of RsmZ(1-72)/RsmE(dimer) 1to3 complex
2MF1 の概要
エントリーDOI | 10.2210/pdb2mf1/pdb |
関連するPDBエントリー | 2MF0 |
分子名称 | Carbon storage regulator homolog, RNA_(72-MER) (2 entities in total) |
機能のキーワード | protein/rna, non-coding rna, translation repressor protein, pseudomonas aeruginosa, messenger rna, protein sequestration, two conformations, rnase e cleave sites, homo-dimeric proteins, cooperativity, multiple protein binding sites, translation activation, ribosome binding site, large solution structure, electron paramagnetic resonance, protein sponge, rnp assembly, rna binding protein-rna complex, rna binding protein/rna |
由来する生物種 | Pseudomonas protegens Pf-5 |
タンパク質・核酸の鎖数 | 7 |
化学式量合計 | 70459.74 |
構造登録者 | Duss, O.,Michel, E.,Yulikov, M.,Schubert, M.,Jeschke, G.,Allain, F.H.-T. (登録日: 2013-10-02, 公開日: 2014-05-21, 最終更新日: 2024-05-01) |
主引用文献 | Duss, O.,Michel, E.,Yulikov, M.,Schubert, M.,Jeschke, G.,Allain, F.H. Structural basis of the non-coding RNA RsmZ acting as a protein sponge. Nature, 509:588-592, 2014 Cited by PubMed Abstract: MicroRNA and protein sequestration by non-coding RNAs (ncRNAs) has recently generated much interest. In the bacterial Csr/Rsm system, which is considered to be the most general global post-transcriptional regulatory system responsible for bacterial virulence, ncRNAs such as CsrB or RsmZ activate translation initiation by sequestering homodimeric CsrA-type proteins from the ribosome-binding site of a subset of messenger RNAs. However, the mechanism of ncRNA-mediated protein sequestration is not understood at the molecular level. Here we show for Pseudomonas fluorescens that RsmE protein dimers assemble sequentially, specifically and cooperatively onto the ncRNA RsmZ within a narrow affinity range. This assembly yields two different native ribonucleoprotein structures. Using a powerful combination of nuclear magnetic resonance and electron paramagnetic resonance spectroscopy we elucidate these 70-kilodalton solution structures, thereby revealing the molecular mechanism of the sequestration process and how RsmE binding protects the ncRNA from RNase E degradation. Overall, our findings suggest that RsmZ is well-tuned to sequester, store and release RsmE and therefore can be viewed as an ideal protein 'sponge'. PubMed: 24828038DOI: 10.1038/nature13271 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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