5YKO

Crystal structure of Arabidopsis thaliana JMJ14 catalytic domain in complex with NOG and H3K4me3 peptide

5YKO の概要

• エントリーDOI: 10.2210/pdb5yko/pdb
• 分子名称: Probable lysine-specific demethylase JMJ14, H3(1-10)K4me3 peptide, NICKEL (II) ION, ... (5 entities in total)
• 機能のキーワード: jmj14, jumonji domain, c5hc2 zinc finger, h3k4me3 demethylase, gene regulation
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• 細胞内の位置: Nucleus, nucleoplasm : Q8GUI6; Nucleus : P59226
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66530.84

構造登録者

Yang, Z.,Du, J. (登録日: 2017-10-15, 公開日: 2017-12-27, 最終更新日: 2023-11-22)

主引用文献

Yang, Z.,Qiu, Q.,Chen, W.,Jia, B.,Chen, X.,Hu, H.,He, K.,Deng, X.,Li, S.,Tao, W.A.,Cao, X.,Du, J.
Structure of the Arabidopsis JMJ14-H3K4me3 Complex Provides Insight into the Substrate Specificity of KDM5 Subfamily Histone Demethylases.
Plant Cell, 30:167-177, 2018

PubMed Abstract: In chromatin, histone methylation affects the epigenetic regulation of multiple processes in animals and plants and is modulated by the activities of histone methyltransferases and histone demethylases. The jumonji domain-containing histone demethylases have diverse functions and can be classified into several subfamilies. In humans, the jumonji domain-containing Lysine (K)-Specific Demethylase 5/Jumonji and ARID Domain Protein (KDM5/JARID) subfamily demethylases are specific for histone 3 lysine 4 trimethylation (H3K4me3) and are important drug targets for cancer treatment. In , the KDM5/JARID subfamily H3K4me3 demethylase JUMONJI14 (JMJ14) plays important roles in flowering, gene silencing, and DNA methylation. Here, we report the crystal structures of the JMJ14 catalytic domain in both substrate-free and bound forms. The structures reveal that the jumonji and C5HC2 domains contribute to the specific recognition of the H3R2 and H3Q5 to facilitate H3K4me3 substrate specificity. The critical acidic residues are conserved in plants and animals with the corresponding mutations impairing the enzyme activity of both JMJ14 and human KDM5B, indicating a common substrate recognition mechanism for KDM5 subfamily demethylases shared by plants and animals and further informing efforts to design targeted inhibitors of human KDM5.

PubMed: 29233856
DOI: 10.1105/tpc.17.00666

実験手法

X-RAY DIFFRACTION (2.9 Å)