9CA7

Cryo-EM structure of human SRCAP-nucleosome complex in the fully-engaged state (composite structure)

これはPDB形式変換不可エントリーです。

9CA7 の概要

• エントリーDOI: 10.2210/pdb9ca7/pdb
• EMDBエントリー: 45381
• 分子名称: Helicase SRCAP, Histone H4, DNA (285-MER), ... (16 entities in total)
• 機能のキーワード: chromatin remodeler, snf2 family atpase, h2a.z, gene regulation
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 1041106.15

構造登録者

Louder, R.K.,Park, G. (登録日: 2024-06-17, 公開日: 2025-06-18, 最終更新日: 2026-08-12)

主引用文献

Park, G.,Wu, C.,Louder, R.K.
Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme.
Sci Adv, 12:eaei7728-eaei7728, 2026

PubMed Abstract: The conserved yeast SWR1 and human SRCAP chromatin remodeling complexes catalyze exchange of nucleosomal histone H2A for H2A.Z, but the underlying mechanism has remained obscure. Here, we show that histone exchange by SRCAP requires the transient activator CFDP1 and resolve nine cryo-electron microscopy structures of the SRCAP-CFDP1 holoenzyme that define the stepwise exchange mechanism. CFDP1 recognizes the conformation of the fully engaged SRCAP-nucleosome complex through interactions with multiple subunits-including direct contact with the ATPase domain-and induces conformational transitions that drive extensive DNA unwrapping, eviction of the H2A-H2B dimer, and insertion of the H2A.Z-H2B dimer, all without necessarily requiring hydrolysis of bound ATP. Collectively, these findings provide unprecedented insight into the mechanism of activator- and nucleotide-driven histone exchange from nucleosomal H2A to H2A.Z.

PubMed: 42536744
DOI: 10.1126/sciadv.aei7728

実験手法

ELECTRON MICROSCOPY (3.35 Å)