5IZW
Crystal structure of RNA editing specific factor of designer PLS-type PPR-9R protein
Summary for 5IZW
| Entry DOI | 10.2210/pdb5izw/pdb |
| Descriptor | PLS9-PPR (2 entities in total) |
| Functional Keywords | pentatricopeptide repeat, complex, morf, rna binding protein |
| Biological source | unidentified |
| Total number of polymer chains | 2 |
| Total formula weight | 22534.14 |
| Authors | |
| Primary citation | Yan, J.,Zhang, Q.,Guan, Z.,Wang, Q.,Li, L.,Ruan, F.,Lin, R.,Zou, T.,Yin, P. MORF9 increases the RNA-binding activity of PLS-type pentatricopeptide repeat protein in plastid RNA editing Nat Plants, 3:17037-17037, 2017 Cited by PubMed Abstract: RNA editing is a post-transcriptional process that modifies the genetic information on RNA molecules. In flowering plants, RNA editing usually alters cytidine to uridine in plastids and mitochondria. The PLS-type pentatricopeptide repeat (PPR) protein and the multiple organellar RNA editing factor (MORF, also known as RNA editing factor interacting protein (RIP)) are two types of key trans-acting factors involved in this process. However, how they cooperate with one another remains unclear. Here, we have characterized the interactions between a designer PLS-type PPR protein (PLS)PPR and MORF9, and found that RNA-binding activity of (PLS)PPR is drastically increased on MORF9 binding. We also determined the crystal structures of (PLS)PPR, MORF9 and the (PLS)PPR-MORF9 complex. MORF9 binding induces significant compressed conformational changes of (PLS)PPR, revealing the molecular mechanisms by which MORF9-bound (PLS)PPR has increased RNA-binding activity. Similarly, increased RNA-binding activity is observed for the natural PLS-type PPR protein, LPA66, in the presence of MORF9. These findings significantly expand our understanding of MORF function in plant organellar RNA editing. PubMed: 28394309DOI: 10.1038/nplants.2017.37 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.738 Å) |
Structure validation
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