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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Binding Sites
-
Catalysis
-
Computer Graphics
-
Crystallography, X-Ray
-
DNA Glycosylases*
-
DNA Repair*
-
Herpesvirus 1, Human / enzymology*
-
Humans
-
Models, Molecular
-
Molecular Sequence Data
-
N-Glycosyl Hydrolases / chemistry
-
N-Glycosyl Hydrolases / metabolism*
-
Protein Structure, Secondary
-
Structure-Activity Relationship
-
Substrate Specificity
-
Thymine / metabolism
-
Uracil / metabolism*
-
Uracil-DNA Glycosidase
Substances
-
Uracil
-
DNA Glycosylases
-
N-Glycosyl Hydrolases
-
Uracil-DNA Glycosidase
-
Thymine