4C05

Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with SAH

4C05 の概要

• エントリーDOI: 10.2210/pdb4c05/pdb
• 関連するPDBエントリー: 4C03 4C04 4C06 4C07 4C08
• 分子名称: PROTEIN ARGININE N-METHYLTRANSFERASE 6, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• 細胞内の位置: Nucleus : Q6NZB1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42706.20

構造登録者

Bonnefond, L.,Cura, V.,Troffer-Charlier, N.,Mailliot, J.,Wurtz, J.M.,Cavarelli, J. (登録日: 2013-07-31, 公開日: 2014-07-30, 最終更新日: 2025-12-10)

主引用文献

Bonnefond, L.,Stojko, J.,Mailliot, J.,Troffer-Charlier, N.,Cura, V.,Wurtz, J.M.,Cianferani, S.,Cavarelli, J.
Functional Insights from High Resolution Structures of Mouse Protein Arginine Methyltransferase 6.
J.Struct.Biol., 191:175-, 2015

PubMed Abstract: PRMT6 is a protein arginine methyltransferase involved in transcriptional regulation, human immunodeficiency virus pathogenesis, DNA base excision repair, and cell cycle progression. Like other PRMTs, PRMT6 is overexpressed in several cancer types and is therefore considered as a potential anti-cancer drug target. In the present study, we described six crystal structures of PRMT6 from Mus musculus, solved and refined at 1.34 Å for the highest resolution structure. The crystal structures revealed that the folding of the helix αX is required to stabilize a productive active site before methylation of the bound peptide can occur. In the absence of cofactor, metal cations can be found in the catalytic pocket at the expected position of the guanidinium moiety of the target arginine substrate. Using mass spectrometry under native conditions, we show that PRMT6 dimer binds two cofactor and a single H4 peptide molecules. Finally, we characterized a new site of in vitro automethylation of mouse PRMT6 at position 7.

PubMed: 26094878
DOI: 10.1016/J.JSB.2015.06.017

実験手法

X-RAY DIFFRACTION (2.195 Å)