3R0Q

A Uniquely Open Conformation Revealed in the Crystal Structure of Arabidopsis Thaliana Protein Arginine Methyltransferase 10

3R0Q の概要

• エントリーDOI: 10.2210/pdb3r0q/pdb
• 分子名称: Probable protein arginine N-methyltransferase 4.2, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: arginine methyltransferase, methylation, transferase
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 171256.33

構造登録者

Cheng, Y.,Redinbo, M.R. (登録日: 2011-03-08, 公開日: 2011-10-19, 最終更新日: 2024-02-21)

主引用文献

Cheng, Y.,Frazier, M.,Lu, F.,Cao, X.,Redinbo, M.R.
Crystal structure of the plant epigenetic protein arginine methyltransferase 10.
J.Mol.Biol., 414:106-122, 2011

PubMed Abstract: Protein arginine methyltransferase 10 (PRMT10) is a type I arginine methyltransferase that is essential for regulating flowering time in Arabidopsis thaliana. We present a 2.6 Å resolution crystal structure of A. thaliana PRMT 10 (AtPRMT10) in complex with a reaction product, S-adenosylhomocysteine. The structure reveals a dimerization arm that is 12-20 residues longer than PRMT structures elucidated previously; as a result, the essential AtPRMT10 dimer exhibits a large central cavity and a distinctly accessible active site. We employ molecular dynamics to examine how dimerization facilitates AtPRMT10 motions necessary for activity, and we show that these motions are conserved in other PRMT enzymes. Finally, functional data reveal that the 10 N-terminal residues of AtPRMT10 influence substrate specificity, and that enzyme activity is dependent on substrate protein sequences distal from the methylation site. Taken together, these data provide insights into the molecular mechanism of AtPRMT10, as well as other members of the PRMT family of enzymes. They highlight differences between AtPRMT10 and other PRMTs but also indicate that motions are a conserved element of PRMT function.

PubMed: 21986201
DOI: 10.1016/j.jmb.2011.09.040

実験手法

X-RAY DIFFRACTION (2.61 Å)