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The structural basis of specific base-excision repair by uracil-DNA glycosylase
R Savva1, K McAuley-Hecht, T Brown
1Department of Biochemistry and Molecular Biology, University College London, UK.
Nature
|February 9, 1995
Abstract:
The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-1 reveals a new fold, distantly related to dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and with uracil, define the DNA-binding site and allow a detailed understanding of the exquisitely specific recognition of uracil in DNA. The overall structure suggests binding models for elongated single- and double-stranded DNA substrates. Conserved residues close to the uracil-binding site suggest a catalytic mechanism for hydrolytic base excision.