5IZW

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

5IZW の概要

• エントリーDOI: 10.2210/pdb5izw/pdb
• 分子名称: PLS9-PPR (2 entities in total)
• 機能のキーワード: pentatricopeptide repeat, complex, morf, rna binding protein
• 由来する生物種: unidentified
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22534.14

構造登録者

Yan, J.,Zhang, Q.,Guan, Z.,Zou, T.,Yin, P. (登録日: 2016-03-26, 公開日: 2017-03-29, 最終更新日: 2024-03-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.738 Å)