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

Journal article

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.

Authors: Savva, R; McAuley-Hecht, K; Brown, T; Pearl, L

• Publication status: Published
• Journal: Nature
• Volume: 373
• Issue: 6514
• Pages: 487-493
• Publication date: 1995-02-01
• DOI: 10.1038/373487a0
• EISSN: 1476-4687
• ISSN: 0028-0836
• Language: English
• Keywords: N-Glycosyl Hydrolases; DNA Repair; Uracil-DNA Glycosidase; Herpesvirus 1, Human; Catalysis; Binding Sites; Models, Molecular; Humans; Substrate Specificity; Uracil; DNA Glycosylases; Structure-Activity Relationship; Computer Graphics; Protein Structure, Secondary; Thymine; Crystallography, X-Ray; Amino Acid Sequence; Molecular Sequence Data