9CVC

CDAN1 dimer with three ASF1A

9CVC の概要

• エントリーDOI: 10.2210/pdb9cvc/pdb
• EMDBエントリー: 45959
• 分子名称: Codanin-1, Histone chaperone ASF1A (2 entities in total)
• 機能のキーワード: cytosolic, mif4g, histone chaperone, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 361023.66

構造登録者

Sedor, S.F.,Shao, S. (登録日: 2024-07-29, 公開日: 2025-03-26, 最終更新日: 2025-04-02)

主引用文献

Sedor, S.F.,Shao, S.
Mechanism of ASF1 engagement by CDAN1.
Nat Commun, 16:2599-2599, 2025

PubMed Abstract: Codanin-1 (CDAN1) is an essential and ubiquitous protein named after congenital dyserythropoietic anemia type I, an autosomal recessive disease that manifests from mutations in CDAN1 or CDIN1 (CDAN1 interacting nuclease 1). CDAN1 interacts with CDIN1 and the paralogous histone H3-H4 chaperones ASF1A (Anti-Silencing Function 1 A) and ASF1B. However, CDAN1 function remains unclear. Here, we analyze CDAN1 complexes using biochemistry, single-particle cryo-EM, and structural predictions. We find that CDAN1 dimerizes and assembles into cytosolic complexes with CDIN1 and multiple copies of ASF1A/B. One CDAN1 can engage two ASF1 through two B-domains commonly found in ASF1 binding partners and two helices that mimic histone H3 binding. We additionally show that ASF1A and ASF1B have different requirements for CDAN1 engagement. Our findings explain how CDAN1 sequesters ASF1A/B by occupying all functional binding sites known to facilitate histone chaperoning and provide molecular-level insights into this enigmatic complex.

PubMed: 40091041
DOI: 10.1038/s41467-025-57950-z

実験手法

ELECTRON MICROSCOPY (3.5 Å)