1UDG: The Structural Basis Of Specific Base Excision Repair By Uracil-Dna Glycosylase

Citation:
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.
PDB ID: 1UDGDownload
MMDB ID: 57549
PDB Deposition Date: 1995/6/23
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.75  Å
Source Organism:
Similar Structures:
Biological Unit for 1UDG: monomeric; determined by author
Molecular Components in 1UDG
Label Count Molecule
Protein (1 molecule)
1
Uracil-dna Glycosylase(Gene symbol: UL2)
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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