3V6P
Crystal structure of the DNA-binding domain of dHax3, a TAL effector
3V6P の概要
エントリーDOI | 10.2210/pdb3v6p/pdb |
関連するPDBエントリー | 3V6T |
分子名称 | dHax3 (2 entities in total) |
機能のキーワード | 11 tandem repeats, sequence specific dna recognition protein, dna binding protein |
由来する生物種 | Xanthomonas |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 45884.54 |
構造登録者 | |
主引用文献 | Deng, D.,Yan, C.Y.,Pan, X.J.,Mahfouz, M.,Wang, J.W.,Zhu, J.K.,Shi, Y.G.,Yan, N. Structural Basis for Sequence-Specific Recognition of DNA by TAL Effectors Science, 2012 Cited by PubMed Abstract: TAL (transcription activator-like) effectors, secreted by phytopathogenic bacteria, recognize host DNA sequences through a central domain of tandem repeats. Each repeat comprises 33 to 35 conserved amino acids and targets a specific base pair by using two hypervariable residues [known as repeat variable diresidues (RVDs)] at positions 12 and 13. Here, we report the crystal structures of an 11.5-repeat TAL effector in both DNA-free and DNA-bound states. Each TAL repeat comprises two helices connected by a short RVD-containing loop. The 11.5 repeats form a right-handed, superhelical structure that tracks along the sense strand of DNA duplex, with RVDs contacting the major groove. The 12th residue stabilizes the RVD loop, whereas the 13th residue makes a base-specific contact. Understanding DNA recognition by TAL effectors may facilitate rational design of DNA-binding proteins with biotechnological applications. PubMed: 22223738DOI: 10.1126/science.1215670 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.401 Å) |
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