Homing Endonuclease I-TevI: An Atypical Zinc Finger with a Novel Function
Zinc Finger Proteins(2005)
摘要
I-TevI is a site-specific, sequence-tolerant homing endonuclease encoded by thetdintron of bacteriophage T4. The enzyme consists of an N-terminal catalytic domain and a C-terminal DNA-binding domain that are connected by a long, flexible linker. The crystal structure of the DNA-binding domain of I-TevI, residues 130 to 245, complexed with the 20-bp primary binding region of its DNA target, reveals the presence of a zinc finger, comprising residues 151 to 167, that makes backbone contacts with the DNA from the minor groove. Biochemical data have shown that the zinc finger does not contribute to the DNA-binding affinity or to the specificity of the enzyme, but rather that it has a novel function and acts as a distance determinant that controls the relative positions of the catalytic and DNA-binding domains.
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