3B3F

The 2.2 A crystal structure of the catalytic domain of coactivator-associated arginine methyl transferase I(CARM1,142-478), in complex with S-adenosyl homocysteine

3B3F の概要

• エントリーDOI: 10.2210/pdb3b3f/pdb
• 関連するPDBエントリー: 2OQB 3B3G 3B3J
• 分子名称: Histone-arginine methyltransferase CARM1, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: protein arginine methyltransferase, catalytic domain, chromatin regulator, mrna processing, mrna splicing, nucleus, s-adenosyl-l-methionine, transcription, transcription regulation, transferase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Nucleus: Q4AE70
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 156634.28

構造登録者

Troffer-Charlier, N.,Cura, V.,Hassenboehler, P.,Moras, D.,Cavarelli, J. (登録日: 2007-10-22, 公開日: 2007-11-06, 最終更新日: 2024-02-21)

主引用文献

Troffer-Charlier, N.,Cura, V.,Hassenboehler, P.,Moras, D.,Cavarelli, J.
Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains.
Embo J., 26:4391-4401, 2007

PubMed Abstract: Coactivator-associated arginine methyltransferase 1 (CARM1), a protein arginine methyltransferase recruited by several transcription factors, methylates a large variety of proteins and plays a critical role in gene expression. We report, in this paper, four crystal structures of isolated modules of CARM1. The 1.7 A crystal structure of the N-terminal domain of CARM1 reveals an unexpected PH domain, a scaffold frequently found to regulate protein-protein interactions in a large variety of biological processes. Three crystal structures of the CARM1 catalytic module, two free and one cofactor-bound forms (refined at 2.55 A, 2.4 A and 2.2 A, respectively) reveal large structural modifications including disorder to order transition, helix to strand transition and active site modifications. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may inspire how CARM1 regulates its biological activities by protein-protein interactions.

PubMed: 17882262
DOI: 10.1038/sj.emboj.7601855

実験手法

X-RAY DIFFRACTION (2.2 Å)