The structural basis of specific base-excision repair by uracil-DNA glycosylase.
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.
Department of Biochemistry and Molecular Biology, University College London, UK.
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Savva
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McAuley-Hecht
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Brown
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Pearl
D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D045647:DNA Glycosylases; D004260:DNA Repair; D018259:Herpesvirus 1, Human / Q000201:enzymology*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000737:chemistry / Q000378:metabolism*; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013941:Thymine / Q000378:metabolism; D014498:Uracil / Q000378:metabolism*; D051981:Uracil-DNA Glycosidase
D014498:Uracil; D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases; D051981:Uracil-DNA Glycosidase; D013941:Thymine