3V6P: Crystal Structure Of The Dna-Binding Domain Of Dhax3, A Tal Effector

TAL 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 using two hypervariable residues (known as RVD) at positions 12 and 13. Here, we report the crystal structures of a 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, super-helical 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.
PDB ID: 3V6PDownload
MMDB ID: 96574
PDB Deposition Date: 2011/12/20
Updated in MMDB: 2012/01
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 3V6P: monomeric; determined by author and by software (PISA)
Molecular Components in 3V6P
Label Count Molecule
Protein (1 molecule)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB