3V6T
Crystal structure of the DNA-bound dHax3, a TAL effector, at 1.85 angstrom
Summary for 3V6T
Entry DOI | 10.2210/pdb3v6t/pdb |
Related | 3V6P |
Descriptor | dHax3, DNA (5'-D(*TP*GP*TP*CP*CP*CP*TP*TP*TP*AP*TP*CP*TP*CP*TP*CP*T)-3'), DNA (5'-D(*AP*GP*AP*GP*AP*GP*AP*TP*AP*AP*AP*GP*GP*GP*AP*CP*A)-3'), ... (4 entities in total) |
Functional Keywords | 11 tandem repeats, dna specific binding protein, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Xanthomonas |
Total number of polymer chains | 6 |
Total formula weight | 124298.53 |
Authors | |
Primary citation | 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 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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