3S8P

Crystal Structure of the SET Domain of Human Histone-Lysine N-Methyltransferase SUV420H1 In Complex With S-Adenosyl-L-Methionine

3S8P の概要

• エントリーDOI: 10.2210/pdb3s8p/pdb
• 分子名称: Histone-lysine N-methyltransferase SUV420H1, ZINC ION, S-ADENOSYLMETHIONINE, ... (4 entities in total)
• 機能のキーワード: set domain, histone methyltransferase, transcription regulation, histone lysine, sam, methylation, nucleus, chromosome, structural genomics, structural genomics consortium, sgc, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : Q4FZB7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64689.94

構造登録者

Lam, R.,Zeng, H.,Loppnau, P.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Wu, H.,Structural Genomics Consortium (SGC) (登録日: 2011-05-30, 公開日: 2011-07-06, 最終更新日: 2024-11-20)

主引用文献

Wu, H.,Siarheyeva, A.,Zeng, H.,Lam, R.,Dong, A.,Wu, X.H.,Li, Y.,Schapira, M.,Vedadi, M.,Min, J.
Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2.
Febs Lett., 587:3859-3868, 2013

PubMed Abstract: SUV420H1 and SUV420H2 are two highly homologous enzymes that methylate lysine 20 of histone H4 (H4K20), a mark that has been implicated in transcriptional regulation. In this study, we present the high-resolution crystal structures of human SUV420H1 and SUV420H2 in complex with SAM, and report their substrate specificity. Both methyltransferases have a unique N-terminal domain and Zn-binding post-SET domain, and prefer the monomethylated histone H4K20 as a substrate in vitro. No histone H4K20 trimethylation activity was detected by our radioactivity-based assay for either enzyme, consistent with the presence of a conserved serine residue that forms a hydrogen bond with the target lysine side-chain and limits the methylation level.

PubMed: 24396869

実験手法

X-RAY DIFFRACTION (1.85 Å)