6PWV

Cryo-EM structure of MLL1 core complex bound to the nucleosome

これはPDB形式変換不可エントリーです。

6PWV の概要

• エントリーDOI: 10.2210/pdb6pwv/pdb
• EMDBエントリー: 20512
• 分子名称: Retinoblastoma-binding protein 5, Protein dpy-30 homolog, Set1/Ash2 histone methyltransferase complex subunit ASH2, ... (13 entities in total)
• 機能のキーワード: mixed-lineage leukemia, mll1, nucleosome, histone h3 lys4 methyltransferase, rbbp5, wdr5, histone binding-dna binding-dna complex, histone binding/dna binding/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 401256.02

構造登録者

Park, S.H.,Ayoub, A.,Lee, Y.T.,Xu, J.,Zhang, W.,Zhang, B.,Zhang, Y.,Cianfrocco, M.A.,Su, M.,Dou, Y.,Cho, U. (登録日: 2019-07-23, 公開日: 2019-12-18, 最終更新日: 2023-08-16)

主引用文献

Park, S.H.,Ayoub, A.,Lee, Y.T.,Xu, J.,Kim, H.,Zheng, W.,Zhang, B.,Sha, L.,An, S.,Zhang, Y.,Cianfrocco, M.A.,Su, M.,Dou, Y.,Cho, U.S.
Cryo-EM structure of the human MLL1 core complex bound to the nucleosome.
Nat Commun, 10:5540-5540, 2019

PubMed Abstract: Mixed lineage leukemia (MLL) family histone methyltransferases are enzymes that deposit histone H3 Lys4 (K4) mono-/di-/tri-methylation and regulate gene expression in mammals. Despite extensive structural and biochemical studies, the molecular mechanisms whereby the MLL complexes recognize histone H3K4 within nucleosome core particles (NCPs) remain unclear. Here we report the single-particle cryo-electron microscopy (cryo-EM) structure of the NCP-bound human MLL1 core complex. We show that the MLL1 core complex anchors to the NCP via the conserved RbBP5 and ASH2L, which interact extensively with nucleosomal DNA and the surface close to the N-terminal tail of histone H4. Concurrent interactions of RbBP5 and ASH2L with the NCP uniquely align the catalytic MLL1 domain at the nucleosome dyad, thereby facilitating symmetrical access to both H3K4 substrates within the NCP. Our study sheds light on how the MLL1 complex engages chromatin and how chromatin binding promotes MLL1 tri-methylation activity.

PubMed: 31804488
DOI: 10.1038/s41467-019-13550-2

実験手法

ELECTRON MICROSCOPY (6.2 Å)