5CVE

Crystal Structure of human NRMT1 in complex with dimethylated fly H2B peptide and SAH

5CVE の概要

• エントリーDOI: 10.2210/pdb5cve/pdb
• 関連するPDBエントリー: 5CVD
• 分子名称: N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminal peptide from Histone H2B, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• 機能のキーワード: n-terminal methyltransferase, transferase-peptide complex, transferase/peptide
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q9BV86 P02283
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57721.77

構造登録者

Wu, R.,Li, H. (登録日: 2015-07-26, 公開日: 2015-11-25, 最終更新日: 2025-04-09)

主引用文献

Wu, R.,Yue, Y.,Zheng, X.,Li, H.
Molecular basis for histone N-terminal methylation by NRMT1
Genes Dev., 29:2337-2342, 2015

PubMed Abstract: NRMT1 is an N-terminal methyltransferase that methylates histone CENP-A as well as nonhistone substrates. Here, we report the crystal structure of human NRMT1 bound to CENP-A peptide at 1.3 Å. NRMT1 adopts a core methyltransferase fold that resembles DOT1L and PRMT but not SET domain family histone methyltransferases. Key substrate recognition and catalytic residues were identified by mutagenesis studies. Histone peptide profiling revealed that human NRMT1 is highly selective to human CENP-A and fruit fly H2B, which share a common "Xaa-Pro-Lys/Arg" motif. These results, along with a 1.5 Å costructure of human NRMT1 bound to the fruit fly H2B peptide, underscore the importance of the NRMT1 recognition motif.

PubMed: 26543159
DOI: 10.1101/gad.270926.115

実験手法

X-RAY DIFFRACTION (1.5 Å)