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5IZW

Crystal structure of RNA editing specific factor of designer PLS-type PPR-9R protein

Summary for 5IZW
Entry DOI10.2210/pdb5izw/pdb
DescriptorPLS9-PPR (2 entities in total)
Functional Keywordspentatricopeptide repeat, complex, morf, rna binding protein
Biological sourceunidentified
Total number of polymer chains2
Total formula weight22534.14
Authors
Yan, J.,Zhang, Q.,Guan, Z.,Zou, T.,Yin, P. (deposition date: 2016-03-26, release date: 2017-03-29, Last modification date: 2024-03-20)
Primary citationYan, 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: 28394309
DOI: 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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