G:U mismatches resulting from deamination of cytosine are the most common 
promutagenic lesions occurring in DNA. Uracil is removed in a base-excision 
repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both 
single- and double-stranded DNA. Recently, a biochemically distinct family of 
DNA repair enzymes has been identified, which excises both uracil and thymine, 
but only from mispairs with guanine. Crystal structures of the mismatch-specific 
uracil DNA-glycosylase (MUG) from E. coli, and of a DNA complex, reveal a 
remarkable structural and functional homology to UDGs despite low sequence 
identity. Details of the MUG structure explain its thymine DNA-glycosylase 
activity and the specificity for G:U/T mispairs, which derives from direct 
recognition of guanine on the complementary strand.