5MPW

Crystal structure of Arabidopsis thaliana RNA editing factor MORF1

5MPW の概要

• エントリーDOI: 10.2210/pdb5mpw/pdb
• 分子名称: Multiple organellar RNA editing factor 1, mitochondrial, BROMIDE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: nfld-related fold, plant protein
• 由来する生物種: Arabidopsis thaliana (Thale cress)
• 細胞内の位置: Mitochondrion : O49429
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 54531.68

構造登録者

Haag, S.,Schindler, M.,Berndt, L.,Brennicke, A.,Takenaka, M.,Weber, G. (登録日: 2016-12-19, 公開日: 2017-02-22, 最終更新日: 2024-11-20)

主引用文献

Haag, S.,Schindler, M.,Berndt, L.,Brennicke, A.,Takenaka, M.,Weber, G.
Crystal structures of the Arabidopsis thaliana organellar RNA editing factors MORF1 and MORF9.
Nucleic Acids Res., 45:4915-4928, 2017

PubMed Abstract: In flowering plant plastids and mitochondria, multiple organellar RNA editing factor (MORF/RIP) proteins are required at most sites for efficient C to U RNA editing catalyzed by the RNA editosome. MORF proteins harbor a conserved stretch of residues (MORF-box), form homo- and heteromers and interact with selected PPR (pentatricopeptide repeat) proteins, which recognize each editing site. The molecular function of the MORF-box remains elusive since it shares no sequence similarity with known domains. We determined structures of the A. thaliana mitochondrial MORF1 and chloroplast MORF9 MORF-boxes which both adopt a novel globular fold (MORF domain). Our structures state a paradigmatic model for MORF domains and their specific dimerization via a hydrophobic interface. We cross-validate the interface by yeast two-hybrid studies and pulldown assays employing structure-based mutants. We find a structural similarity of the MORF domain to an N-terminal ferredoxin-like domain (NFLD), which confers RNA substrate positioning in bacterial 4-thio-uracil tRNA synthetases, implying direct RNA contacts of MORF proteins during RNA editing. With the MORF1 and MORF9 structures we elucidate a yet unknown fold, corroborate MORF interaction studies, validate the mechanism of MORF multimerization by structure-based mutants and pave the way towards a complete structural characterization of the plant RNA editosome.

PubMed: 28201607
DOI: 10.1093/nar/gkx099

実験手法

X-RAY DIFFRACTION (1.499 Å)