Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues

We report the first high-resolution structures of TDG in an enzyme-substrate complex, for G·U bound to TDG82-308 (1.54 Å) and TDG111-308 (1.71 Å), revealing new enzyme-substrate contacts, direct and water-mediated. We also report a structure of the TDG82-308 product complex (1.70 Å). TDG82-308 forms unique enzyme–DNA interactions, supporting its value for structure-function studies. The results advance understanding of how TDG recognizes and removes modified bases from DNA, particularly those resulting from deamination.

Source: Nucleic Acids Research - December 1, 2016 Category: Research Authors: Coey, C. T., Malik, S. S., Pidugu, L. S., Varney, K. M., Pozharski, E., Drohat, A. C. Tags: Genome Integrity, Repair and Replication Source Type: research