4OE1

Crystal structure of the pentatricopeptide repeat protein PPR10 (C256S/C430S/C449S) in complex with an 18-nt PSAJ rna element

4OE1 の概要

• エントリーDOI: 10.2210/pdb4oe1/pdb
• 関連するPDBエントリー: 4M59
• 分子名称: Chloroplast pentatricopeptide repeat protein 10, psaJ RNA, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: pentatricopeptide repeats, superhelical, rna binding protein, rna, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Zea mays (maize)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 169888.83

構造登録者

Li, Q.,Yan, C.,Wu, J.,Yin, P.,Yan, N. (登録日: 2014-01-11, 公開日: 2014-09-24, 最終更新日: 2023-09-20)

主引用文献

Li, Q.,Yan, C.,Xu, H.,Wang, Z.,Long, J.,Li, W.,Wu, J.,Yin, P.,Yan, N.
Examination of the dimerization states of the single-stranded RNA recognition protein pentatricopeptide repeat 10 (PPR10).
J.Biol.Chem., 289:31503-31512, 2014

PubMed Abstract: Pentatricopeptide repeat (PPR) proteins, particularly abundant in plastids and mitochrondria of angiosperms, include a large number of sequence-specific RNA binding proteins that are involved in diverse aspects of organelle RNA metabolisms. PPR proteins contain multiple tandom repeats, and each repeat can specifically recognize a RNA base through residues 2, 5, and 35 in a modular fashion. The crystal structure of PPR10 from maize chloroplast exhibits dimeric existence both in the absence and presence of the 18-nucleotide psaJ RNA element. However, previous biochemical analysis suggested a monomeric shift of PPR10 upon RNA binding. In this report, we show that the amino-terminal segments of PPR10 determine the dimerization state of PPR10. A single amino acid alteration of cysteine to serine within repeat 10 of PPR10 further drives dimerization of PPR10. The biochemical elucidation of the determinants for PPR10 dimerization may provide an important foundation to understand the working mechanisms of PPR proteins underlying their diverse physiological functions.

PubMed: 25231995
DOI: 10.1074/jbc.M114.575472

実験手法

X-RAY DIFFRACTION (2.8 Å)