5IWW

Crystal structure of RNA editing factor of designer PLS-type PPR/9R protein in complex with MORF9/RIP9

Summary for 5IWW

• Entry DOI: 10.2210/pdb5iww/pdb
• Related: 5IW8
• Descriptor: Multiple organellar RNA editing factor 9, chloroplastic, PLS9-PPR (3 entities in total)
• Functional Keywords: pentatricopeptide repeat, complex, morf, pls-type, rna binding protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Cellular location: Plastid, chloroplast : Q9LPZ1
• Total number of polymer chains: 4
• Total formula weight: 85575.31

Authors

Yan, J.,Zhang, Q.,Guan, Z.,Zou, T.,Yin, P. (deposition date: 2016-03-23, release date: 2017-03-29, Last modification date: 2024-03-20)

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

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: 28394309
DOI: 10.1038/nplants.2017.37

Experimental method

X-RAY DIFFRACTION (2.65 Å)