5DST

Crystal structure of human PRMT8 in complex with SAH

5DST の概要

• エントリーDOI: 10.2210/pdb5dst/pdb
• 分子名称: Protein arginine N-methyltransferase 8, S-ADENOSYL-L-HOMOCYSTEINE (2 entities in total)
• 機能のキーワード: methyltransferase, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 583447.57

構造登録者

Toma-Fukai, S.,Shimizu, T. (登録日: 2015-09-17, 公開日: 2016-02-24, 最終更新日: 2024-03-20)

主引用文献

Toma-Fukai, S.,Kim, J.D.,Park, K.E.,Kuwabara, N.,Shimizu, N.,Krayukhina, E.,Uchiyama, S.,Fukamizu, A.,Shimizu, T.
Novel helical assembly in arginine methyltransferase 8
J.Mol.Biol., 428:1197-1208, 2016

PubMed Abstract: Protein arginine methyltransferase 8 (PRMT8) is unique among PRMTs, as it is specifically expressed in brain and localized to the plasma membrane via N-terminal myristoylation. Here, we describe the crystal structure of human PRMT8 (hPRMT8) at 3.0-Å resolution. The crystal structure of hPRMT8 exhibited a novel helical assembly. Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution. This octameric structure is necessary for proper localization to the plasma membrane and efficient methyltransferase activity. The helical assembly might be a relevant quaternary form for hPRMT1, which is the predominant PRMT in mammalian cells and most closely related to hPRMT8.

PubMed: 26876602
DOI: 10.1016/j.jmb.2016.02.007

実験手法

X-RAY DIFFRACTION (2.963 Å)