5YDG

Crystal structure of the Arabidopsis thaliana chloroplast RNA editing factors 2(MORF2)

Summary for 5YDG

• Entry DOI: 10.2210/pdb5ydg/pdb
• Descriptor: Multiple organellar RNA editing factor 2, chloroplastic (2 entities in total)
• Functional Keywords: rna editing, morfs, arabidopsis thaliana, rna binding protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Cellular location: Plastid, chloroplast : O22793
• Total number of polymer chains: 2
• Total formula weight: 26329.55

Authors

Wang, X.,Yang, J.Y.,Wang, Y.L.,Gao, Y.S. (deposition date: 2017-09-13, release date: 2017-12-20, Last modification date: 2024-03-27)

Primary citation

Yang, J.,Zhang, M.,Wang, X.
Crystal structure of the chloroplast RNA editing factor MORF2
Biochem. Biophys. Res. Commun., 495:2038-2043, 2018

PubMed Abstract: RNA editing is a post-transcription process that alters the genetic information on RNA molecules. In plastids and mitochondria of flowering plants, the multiple organellar RNA editing factors (MORFs) interact with the PLS-type pentatricopeptide repeat (PPR) proteins and participate in RNA editing of cytidine-to-uridine conversion. The PPR proteins recognize cytidine targets around the editing sites, and the MORF proteins modulate the RNA-binding activity of the PPR proteins. Here, we report the structure of the Arabidopsis thaliana chloroplast MORF2 at 2.4 Å resolution. The structure, adopting typical MORF-box fold as observed in mitochondrial MORF1 and chloroplast MORF9, reveals an MORF1-like dimerization mode. The difference between the two dimerization modes can be attributed to F157 (corresponding F162 in MORF1 and W160 in MORF9), which causes a 60° shift upon dimerization. This observation, together with the PPR-MORF2 model, suggests a dimer-to-monomer transition during RNA editosome formation.

PubMed: 29229384
DOI: 10.1016/j.bbrc.2017.12.044

Experimental method

X-RAY DIFFRACTION (2.405 Å)