5ZBA

Crystal structure of Rtt109-Asf1-H3-H4-CoA complex

5ZBA の概要

• エントリーDOI: 10.2210/pdb5zba/pdb
• 関連するPDBエントリー: 5ZB9
• 分子名称: DNA damage response protein Rtt109, putative, Histone chaperone asf1, Histone H3, ... (6 entities in total)
• 機能のキーワード: histone, acetylation, chaperone, dna replication, nucleosome assembly, dna damage, transferase, transferase-structural protein complex, transferase/structural protein
• 由来する生物種: Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 113032.22

構造登録者

Zhang, L.,Serra-Cardona, A.,Zhou, H.,Wang, M.,Yang, N.,Zhang, Z.,Xu, R.M. (登録日: 2018-02-10, 公開日: 2018-07-25, 最終更新日: 2023-11-22)

主引用文献

Zhang, L.,Serra-Cardona, A.,Zhou, H.,Wang, M.,Yang, N.,Zhang, Z.,Xu, R.M.
Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.
Cell, 174:818-830.e11, 2018

PubMed Abstract: Rtt109 is a unique histone acetyltransferase acetylating histone H3 lysine 56 (H3K56), a modification critical for DNA replication-coupled nucleosome assembly and genome stability. In cells, histone chaperone Asf1 is essential for H3K56 acetylation, yet the mechanisms for H3K56 specificity and Asf1 requirement remain unknown. We have determined the crystal structure of the Rtt109-Asf1-H3-H4 complex and found that unwinding of histone H3 α, where K56 is normally located, and stabilization of the very C-terminal β strand of histone H4 by Asf1 are prerequisites for H3K56 acetylation. Unexpectedly, an interaction between Rtt109 and the central helix of histone H3 is also required. The observed multiprotein, multisite substrate recognition mechanism among histone modification enzymes provides mechanistic understandings of Rtt109 and Asf1 in H3K56 acetylation, as well as valuable insights into substrate recognition by histone modification enzymes in general.

PubMed: 30057113
DOI: 10.1016/j.cell.2018.07.005

実験手法

X-RAY DIFFRACTION (3.5 Å)