| Literature DB >> 7845459 |
R Savva1, K McAuley-Hecht, T Brown, L Pearl.
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.Entities:
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Year: 1995 PMID: 7845459 DOI: 10.1038/373487a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962