7FDN
Crystal structure of transcription factor WER in complex with EGL3
7FDN の概要
| エントリーDOI | 10.2210/pdb7fdn/pdb |
| 分子名称 | Transcription factor EGL1, SULFATE ION, GLYCEROL, ... (6 entities in total) |
| 機能のキーワード | transcription factor, transcription |
| 由来する生物種 | Arabidopsis thaliana (thale cress) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 43874.37 |
| 構造登録者 | |
| 主引用文献 | Wang, B.,Luo, Q.,Li, Y.,Du, K.,Wu, Z.,Li, T.,Shen, W.H.,Huang, C.H.,Gan, J.,Dong, A. Structural insights into partner selection for MYB and bHLH transcription factor complexes. Nat.Plants, 8:1108-1117, 2021 Cited by PubMed Abstract: MYB and basic helix-loop-helix (bHLH) transcription factors form complexes to regulate diverse metabolic and developmental processes in plants. However, the molecular mechanisms responsible for MYB-bHLH interaction and partner selection remain unclear. Here, we report the crystal structures of three MYB-bHLH complexes (WER-EGL3, CPC-EGL3 and MYB29-MYC3), uncovering two MYB-bHLH interaction modes. WER and CPC are R2R3- and R3-type MYBs, respectively, but interact with EGL3 through their N-terminal R3 domain in a similar mode. A single amino acid of CPC, Met49, is crucial for competition with WER to interact with EGL3. MYB29, a R2R3-type MYB transcription factor, interacts with MYC3 by its C-terminal MYC-interaction motif. The WER-EGL3 and MYB29-MYC3 binding modes are widely applied among MYB-bHLH complexes in Arabidopsis and evolve independently in plants. PubMed: 35995835DOI: 10.1038/s41477-022-01223-w 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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