6LSB

Crystal Structure of DPF domain of MOZ in complex with H3K14bz peptide

6LSB の概要

• エントリーDOI: 10.2210/pdb6lsb/pdb
• 分子名称: Histone acetyltransferase KAT6A, Histone H3, ZINC ION, ... (4 entities in total)
• 機能のキーワード: dpf domain, histone kbz modification, transcription
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17927.43

構造登録者

Li, H.T.,Ren, X.L. (登録日: 2020-01-17, 公開日: 2020-11-18, 最終更新日: 2023-11-29)

主引用文献

Ren, X.,Zhou, Y.,Xue, Z.,Hao, N.,Li, Y.,Guo, X.,Wang, D.,Shi, X.,Li, H.
Histone benzoylation serves as an epigenetic mark for DPF and YEATS family proteins.
Nucleic Acids Res., 49:114-126, 2021

PubMed Abstract: Histone modifications and their functional readout serve as an important mechanism for gene regulation. Lysine benzoylation (Kbz) on histones is a recently identified acylation mark associated with active transcription. However, it remains to be explored whether putative readers exist to recognize this epigenetic mark. Here, our systematic binding studies demonstrated that the DPF and YEATS, but not the Bromodomain family members, are readers for histone Kbz. Co-crystal structural analyses revealed a 'hydrophobic encapsulation' and a 'tip-sensor' mechanism for Kbz readout by DPF and YEATS, respectively. Moreover, the DPF and YEATS family members display subtle yet unique features to create somewhat flexible engagements of different acylation marks. For instance, YEATS2 but not the other YEATS proteins exhibits best preference for Kbz than lysine acetylation and crotonylation due to its wider 'tip-sensor' pocket. The levels of histone benzoylation in cultured cells or in mice are upregulated upon sodium benzoate treatment, highlighting its dynamic regulation. In summary, our work identifies the first readers for histone Kbz and reveals the molecular basis underlying Kbz recognition, thus paving the way for further functional dissections of histone benzoylation.

PubMed: 33290558
DOI: 10.1093/nar/gkaa1130

実験手法

X-RAY DIFFRACTION (2 Å)