@article{168191,
  keywords = {Models, Molecular, Protein Conformation, Base Sequence, DNA, Crystallography, X-Ray, Protein Structure, Tertiary, Bacterial Proteins, Molecular Sequence Data, Virulence Factors, Amino Acid Sequence, Protein Structure, Secondary, DNA-Binding Proteins, Hydrogen Bonding, Chemical Phenomena, Repetitive Sequences, Amino Acid, Xanthomonas},
  author = {Dong Deng and Chuangye Yan and Xiaojing Pan and Magdy Mahfouz and Jiawei Wang and Jian-Kang Zhu and Yigong Shi and Nieng Yan},
  title = {Structural basis for sequence-specific recognition of DNA by TAL effectors},
  abstract = {<p>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.</p>
},
  year = {2012},
  journal = {Science},
  volume = {335},
  pages = {720-3},
  month = {02/2012},
  issn = {1095-9203},
  doi = {10.1126/science.1215670},
  language = {eng},
}