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

Nature volume 373, pages 487–493 (1995)Cite this article

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.

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Author notes

  1. Laurence Pearl: To whom correspondence should be addressed.

Authors and Affiliations

  1. Structural Biochemistry Section, Department of Biochemistry and Molecular Biology, University College London, Gower Street, London, WC1E 6BT, UK

    Renos Savva

  2. Department of Chemistry, University of Edinburgh, King's Buildings, West Main Road, Edinburgh, EH9 3JJ, UK

    Katherine McAuley-Hecht & Tom Brown

Authors
  1. Renos Savva
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  2. Katherine McAuley-Hecht
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  3. Tom Brown
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  4. Laurence Pearl
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Savva, R., McAuley-Hecht, K., Brown, T. et al. The structural basis of specific base-excision repair by uracil–DNA glycosylase. Nature 373, 487–493 (1995). https://doi.org/10.1038/373487a0

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