6PA7

The cryo-EM structure of the human DNMT3A2-DNMT3B3 complex bound to nucleosome.

6PA7 の概要

• エントリーDOI: 10.2210/pdb6pa7/pdb
• EMDBエントリー: 20281 21689
• 分子名称: Histone H3.2, S-ADENOSYL-L-HOMOCYSTEINE, Histone H4, ... (10 entities in total)
• 機能のキーワード: methyltransferase, complex, transferase, transferase-dna complex, transferase/dna
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 541073.19

構造登録者

Xu, T.H.,Liu, M.,Zhou, X.E.,Liang, G.,Zhao, G.,Xu, H.E.,Melcher, K.,Jones, P.A. (登録日: 2019-06-11, 公開日: 2020-06-17, 最終更新日: 2024-03-20)

主引用文献

Xu, T.H.,Liu, M.,Zhou, X.E.,Liang, G.,Zhao, G.,Xu, H.E.,Melcher, K.,Jones, P.A.
Structure of nucleosome-bound DNA methyltransferases DNMT3A and DNMT3B.
Nature, 586:151-155, 2020

PubMed Abstract: CpG methylation by de novo DNA methyltransferases (DNMTs) 3A and 3B is essential for mammalian development and differentiation and is frequently dysregulated in cancer. These two DNMTs preferentially bind to nucleosomes, yet cannot methylate the DNA wrapped around the nucleosome core, and they favour the methylation of linker DNA at positioned nucleosomes. Here we present the cryo-electron microscopy structure of a ternary complex of catalytically competent DNMT3A2, the catalytically inactive accessory subunit DNMT3B3 and a nucleosome core particle flanked by linker DNA. The catalytic-like domain of the accessory DNMT3B3 binds to the acidic patch of the nucleosome core, which orients the binding of DNMT3A2 to the linker DNA. The steric constraints of this arrangement suggest that nucleosomal DNA must be moved relative to the nucleosome core for de novo methylation to occur.

PubMed: 32968275
DOI: 10.1038/s41586-020-2747-1

実験手法

ELECTRON MICROSCOPY (2.94 Å)