9E3A

Cryo-EM structure of PRMT5/WDR77 in complex with 6S complex (pICln PBM local refinement)

9E3A の概要

• エントリーDOI: 10.2210/pdb9e3a/pdb
• EMDBエントリー: 47476
• 分子名称: Protein arginine N-methyltransferase 5, Methylosome protein WDR77, Methylosome subunit pICln (3 entities in total)
• 機能のキーワード: prmt5, methyl transferase, wdr77, arginine, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 136505.86

構造登録者

Jin, C.Y.,Hunkeler, M.,Fischer, E.S. (登録日: 2024-10-23, 公開日: 2025-02-19)

主引用文献

Jin, C.Y.,Hunkeler, M.,Mulvaney, K.M.,Sellers, W.R.,Fischer, E.S.
Substrate adaptors are flexible tethering modules that enhance substrate methylation by the arginine methyltransferase PRMT5.
J.Biol.Chem., 301:108165-108165, 2025

PubMed Abstract: Protein arginine methyltransferase (PRMT) 5 is an essential arginine methyltransferase responsible for the majority of cellular symmetric dimethyl-arginine marks. PRMT5 uses substrate adaptors such as pICln, RIOK1, and COPR5 to recruit and methylate a wide range of substrates. Although the substrate adaptors play important roles in substrate recognition, how they direct PRMT5 activity towards specific substrates remains incompletely understood. Using biochemistry and cryogenic electron microscopy, we show that these adaptors compete for the same binding site on PRMT5. We find that substrate adaptor and substrate complexes are bound to PRMT5 through two peptide motifs, enabling these adaptors to act as flexible tethering modules to enhance substrate methylation. Taken together, our results shed structural and mechanistic light on the PRMT5 substrate adaptor function and the biochemical nature of PRMT5 interactors.

PubMed: 39793893
DOI: 10.1016/j.jbc.2025.108165

実験手法

ELECTRON MICROSCOPY (3.36 Å)