2V7E
Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), unliganded
2V7E の概要
| エントリーDOI | 10.2210/pdb2v7e/pdb |
| 関連するPDBエントリー | 2V74 |
| 分子名称 | HISTONE-ARGININE METHYLTRANSFERASE CARM1, MERCURY (II) ION (3 entities in total) |
| 機能のキーワード | arginine methyltransferase, s-adenosyl-l-methionine, transcription regulation, histone modification, co- activator, methyltransferase, chromatin regulator, nucleus, transferase, transcription |
| 由来する生物種 | MUS MUSCULUS (MOUSE) |
| 細胞内の位置 | Nucleus: Q9WVG6 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 78810.93 |
| 構造登録者 | Yue, W.W.,Hassler, M.,Roe, S.M.,Thompson-Vale, V.,Pearl, L.H. (登録日: 2007-07-30, 公開日: 2007-10-02, 最終更新日: 2024-02-14) |
| 主引用文献 | Yue, W.W.,Hassler, M.,Roe, S.M.,Thompson-Vale, V.,Pearl, L.H. Insights Into Histone Code Syntax from Structural and Biochemical Studies of Carm1 Methyltransferase Embo J., 26:4402-, 2007 Cited by PubMed Abstract: Coactivator-associated arginine methyltransferase (CARM1) is a transcriptional coactivator that methylates Arg17 and Arg26 in histone H3. CARM1 contains a conserved protein arginine methyltransferase (PRMT) catalytic core flanked by unique pre- and post-core regions. The crystal structures of the CARM1 catalytic core in the apo and holo states reveal cofactor-dependent formation of a substrate-binding groove providing a specific access channel for arginine to the active site. The groove is supported by the first eight residues of the post-core region (C-extension), not present in other PRMTs. In vitro methylation assays show that the C-extension is essential for all histone H3 methylation activity, whereas the pre-core region is required for methylation of Arg26, but not Arg17. Kinetic analysis shows Arg17 methylation is potentiated by pre-acetylation of Lys18, and this is reflected in k(cat) rather than K(m). Together with the absence of specificity subsites in the structure, this suggests an electrostatic sensing mechanism for communicating the modification status of vicinal residues as part of the syntax of the 'histone code.' PubMed: 17882261DOI: 10.1038/SJ.EMBOJ.7601856 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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