The structural basis of specific base-excision repair by uracil–DNA glycosylase
- 9 February 1995
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 373 (6514) , 487-493
- https://doi.org/10.1038/373487a0
Abstract
The 1.75-Å 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.Keywords
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