Summary information and primary citation

PDB-id
1lau; SNAP-derived features in text and JSON formats; DNAproDB
Class
hydrolase-DNA
Method
X-ray (1.8 Å)
Summary
Uracil-DNA glycosylase
Reference
Savva R, McAuley-Hecht K, Brown T, Pearl L (1995): "The structural basis of specific base-excision repair by uracil-DNA glycosylase." Nature, 373, 487-493. doi: 10.1038/373487a0.
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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js