期刊
SCIENCE
卷 335, 期 6069, 页码 716-719出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1216211
关键词
-
资金
- NIH [RL1 0CA833133, R01GM098861, R01 GM088277]
- NSF [0820831]
- Searles Scholars Fellowship
- Northwest Genome Engineering Consortium
DNA recognition by TAL effectors is mediated by tandem repeats, each 33 to 35 residues in length, that specify nucleotides via unique repeat-variable diresidues (RVDs). The crystal structure of PthXo1 bound to its DNA target was determined by high-throughput computational structure prediction and validated by heavy-atom derivatization. Each repeat forms a left-handed, two-helix bundle that presents an RVD-containing loop to the DNA. The repeats self-associate to form a right-handed superhelix wrapped around the DNA major groove. The first RVD residue forms a stabilizing contact with the protein backbone, while the second makes a base-specific contact to the DNA sense strand. Two degenerate amino-terminal repeats also interact with the DNA. Containing several RVDs and noncanonical associations, the structure illustrates the basis of TAL effector-DNA recognition.
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