5GNJ
Structure of a transcription factor and DNA complex
5GNJ の概要
| エントリーDOI | 10.2210/pdb5gnj/pdb |
| 分子名称 | Transcription factor MYC2, DNA (5'-D(*AP*GP*GP*AP*AP*CP*AP*CP*GP*TP*GP*AP*CP*CP*C)-3'), DNA (5'-D(*TP*GP*GP*GP*TP*CP*AP*CP*GP*TP*GP*TP*TP*CP*C)-3'), ... (4 entities in total) |
| 機能のキーワード | transcription factor, dna, complex, dna binding protein-dna complex, dna binding protein/dna |
| 由来する生物種 | Arabidopsis thaliana (Mouse-ear cress) 詳細 |
| 細胞内の位置 | Nucleus : Q39204 |
| タンパク質・核酸の鎖数 | 16 |
| 化学式量合計 | 120215.62 |
| 構造登録者 | |
| 主引用文献 | Lian, T.F.,Xu, Y.P.,Li, L.F.,Su, X.D. Crystal Structure of Tetrameric Arabidopsis MYC2 Reveals the Mechanism of Enhanced Interaction with DNA. Cell Rep, 19:1334-1342, 2017 Cited by PubMed Abstract: Jasmonates (JAs) are essential plant hormones that play important roles in the regulation of plant growth and the response to environmental stress. In the JA signaling pathway, the core transcription factors are a class of basic helix-loop-helix (bHLH) proteins, including MYC2, MYC3, and MYC4, that have different regulatory capacities. Here, we report the 2.7 Å crystal structure of the MYC2 bHLH domain complexed with G-box DNA, showing a cis-tetrameric structure. Biochemical assays confirmed that full-length MYC2 forms a stable homo-tetramer both in solution and in DNA-bound states, whereas MYC3 forms only a homodimer. Isothermal titration calorimetry (ITC) assays demonstrated that tetramerization enhanced DNA binding affinity, and fluorescence resonance energy transfer (FRET) assay indicated DNA looping potential of tetrameric MYC2. Luciferase assay further confirmed the importance of tetramerization in transcriptional regulation. Our studies provide a mechanistic explanation for the regulatory differences of MYC transcription factors. PubMed: 28514654DOI: 10.1016/j.celrep.2017.04.057 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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