3U5V
Crystal structure of Max-E47
3U5V の概要
| エントリーDOI | 10.2210/pdb3u5v/pdb |
| 分子名称 | Protein max, Transcription factor E2-alpha chimera, NITRATE ION (3 entities in total) |
| 機能のキーワード | basic helix-loop-helix (bhlh), transcription factor, transcription |
| 由来する生物種 | Mus musculus (mouse, human) 詳細 |
| 細胞内の位置 | Nucleus: P15923 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 9199.50 |
| 構造登録者 | |
| 主引用文献 | Ahmadpour, F.,Ghirlando, R.,De Jong, A.T.,Gloyd, M.,Shin, J.A.,Guarne, A. Crystal structure of the minimalist max-e47 protein chimera. Plos One, 7:e32136-e32136, 2012 Cited by PubMed Abstract: Max-E47 is a protein chimera generated from the fusion of the DNA-binding basic region of Max and the dimerization region of E47, both members of the basic region/helix-loop-helix (bHLH) superfamily of transcription factors. Like native Max, Max-E47 binds with high affinity and specificity to the E-box site, 5'-CACGTG, both in vivo and in vitro. We have determined the crystal structure of Max-E47 at 1.7 Å resolution, and found that it associates to form a well-structured dimer even in the absence of its cognate DNA. Analytical ultracentrifugation confirms that Max-E47 is dimeric even at low micromolar concentrations, indicating that the Max-E47 dimer is stable in the absence of DNA. Circular dichroism analysis demonstrates that both non-specific DNA and the E-box site induce similar levels of helical secondary structure in Max-E47. These results suggest that Max-E47 may bind to the E-box following the two-step mechanism proposed for other bHLH proteins. In this mechanism, a rapid step where protein binds to DNA without sequence specificity is followed by a slow step where specific protein:DNA interactions are fine-tuned, leading to sequence-specific recognition. Collectively, these results show that the designed Max-E47 protein chimera behaves both structurally and functionally like its native counterparts. PubMed: 22389683DOI: 10.1371/journal.pone.0032136 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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