3V6P

Crystal structure of the DNA-binding domain of dHax3, a TAL effector

Summary for 3V6P

• Entry DOI: 10.2210/pdb3v6p/pdb
• Related: 3V6T
• Descriptor: dHax3 (2 entities in total)
• Functional Keywords: 11 tandem repeats, sequence specific dna recognition protein, dna binding protein
• Biological source: Xanthomonas
• Total number of polymer chains: 1
• Total formula weight: 45884.54

Authors

Deng, D.,Yan, C.Y.,Pan, X.J.,Wang, J.W.,Shi, Y.G.,Yan, N. (deposition date: 2011-12-20, release date: 2012-01-18, Last modification date: 2024-03-20)

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

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: 22223738
DOI: 10.1126/science.1215670

Experimental method

X-RAY DIFFRACTION (2.401 Å)