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

    Savva, Renos and McAuley-Hecht, K. and Brown, T. and Pearl, L. (1995) The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 373 (6514), pp. 487-493. ISSN 0028-0836.

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    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.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 14 May 2019 15:29
    Last Modified: 14 May 2019 15:29
    URI: http://eprints.bbk.ac.uk/id/eprint/27534

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