2MF1
Structural basis of the non-coding RNA RsmZ acting as protein sponge: Conformer R of RsmZ(1-72)/RsmE(dimer) 1to3 complex
Summary for 2MF1
| Entry DOI | 10.2210/pdb2mf1/pdb |
| Related | 2MF0 |
| Descriptor | Carbon storage regulator homolog, RNA_(72-MER) (2 entities in total) |
| Functional Keywords | 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 |
| Biological source | Pseudomonas protegens Pf-5 |
| Total number of polymer chains | 7 |
| Total formula weight | 70459.74 |
| Authors | Duss, O.,Michel, E.,Yulikov, M.,Schubert, M.,Jeschke, G.,Allain, F.H.-T. (deposition date: 2013-10-02, release date: 2014-05-21, Last modification date: 2024-05-01) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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