6A58
Structure of histone demethylase REF6
6A58 の概要
エントリーDOI | 10.2210/pdb6a58/pdb |
関連するPDBエントリー | 6A57 |
分子名称 | Lysine-specific demethylase REF6, ZINC ION (3 entities in total) |
機能のキーワード | complex, histone demethylase ref6, dna, zinc finger, dna binding protein |
由来する生物種 | Arabidopsis thaliana (Mouse-ear cress) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 16783.36 |
構造登録者 | |
主引用文献 | Tian, Z.,Li, X.,Li, M.,Wu, W.,Zhang, M.,Tang, C.,Li, Z.,Liu, Y.,Chen, Z.,Yang, M.,Ma, L.,Caba, C.,Tong, Y.,Lam, H.M.,Dai, S.,Chen, Z. Crystal structures of REF6 and its complex with DNA reveal diverse recognition mechanisms. Cell Discov, 6:17-17, 2020 Cited by PubMed Abstract: Relative of Early Flowing 6 (REF6) is a DNA-sequence-specific H3K27me3/2 demethylase that contains four zinc finger (ZnF) domains and targets several thousand genes in . The ZnF domains are essential for binding target genes, but the structural basis remains unclear. Here, we determined crystal structures of the ZnF domains and REF6-DNA complex, revealing a unique REF6-family-specific half-cross-braced ZnF (RCZ) domain and two C2H2-type ZnFs. DNA-binding induces a profound conformational change in the hinge region of REF6. Each REF6 recognizes six bases and DNA methylation reduces the binding affinity. Both the acidic region and basic region are important for the self-association of REF6. The REF6 DNA-binding affinity is determined by the sequence-dependent conformations of DNA and also the cooperativity in different target motifs. The conformational plasticity enables REF6 to function as a global transcriptional regulator that directly binds to many diverse genes, revealing the structural basis for the epigenetic modification recognition. PubMed: 32257379DOI: 10.1038/s41421-020-0150-6 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.57 Å) |
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