alexa The structural basis of specific base-excision repair by uracil-DNA glycosylase.
Chemical Engineering

Chemical Engineering

Journal of Thermodynamics & Catalysis

Author(s): Savva R, McAuleyHecht K, Brown T, Pearl L

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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. This article was published in Nature and referenced in Journal of Thermodynamics & Catalysis

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