9B2U

Haspin bound to H3 tail

9B2U の概要

• エントリーDOI: 10.2210/pdb9b2u/pdb
• EMDBエントリー: 44115
• 分子名称: Histone H3.2, Serine/threonine-protein kinase haspin (2 entities in total)
• 機能のキーワード: haspin, nucleosome, histone, chromatin, h3t3ph, dna binding protein, dna binding protein-transferase complex, dna binding protein/transferase
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56146.61

構造登録者

Hicks, C.W.,Wolberger, C. (登録日: 2024-03-16, 公開日: 2025-01-22, 最終更新日: 2026-02-04)

主引用文献

Hicks, C.W.,Gliech, C.R.,Rahman, S.,Zhang, X.,Eneim, A.S.,Vasquez, S.J.,Holland, A.J.,Wolberger, C.
Haspin kinase binds to a nucleosomal DNA supergroove.
Nat.Struct.Mol.Biol., 32:1030-1037, 2025

PubMed Abstract: Phosphorylation of histone H3 threonine 3 (H3T3) by Haspin recruits the chromosomal passenger complex to the inner centromere and ensures proper cell cycle progression through mitosis. The mechanism by which Haspin binds to nucleosomes to phosphorylate H3T3 is not known. Here we report cryogenic electron microscopy structures of the human Haspin kinase domain bound to a nucleosome. In contrast with previous structures of histone-modifying enzymes, Haspin solely contacts the nucleosomal DNA, inserting into a supergroove formed by apposing major grooves of two DNA gyres. This binding mode provides a plausible mechanism by which Haspin can bind to nucleosomes in a condensed chromatin environment to phosphorylate H3T3. We identify key basic residues in the Haspin kinase domain that are essential for phosphorylation of nucleosomal histone H3 and binding to mitotic chromatin. Our structural data provide notable insight into a histone-modifying enzyme that binds to nucleosomes solely through DNA contacts.

PubMed: 39979508
DOI: 10.1038/s41594-025-01502-y

実験手法

ELECTRON MICROSCOPY (3.64 Å)