Structural highlights
Function
[UNG_HHV11] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly, in terminally differentiated neurons which lack DNA repair enzymes.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The structural basis of specific base-excision repair by uracil-DNA glycosylase.,Savva R, McAuley-Hecht K, Brown T, Pearl L Nature. 1995 Feb 9;373(6514):487-93. PMID:7845459[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Savva R, Pearl LH. Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex. Nat Struct Biol. 1995 Sep;2(9):752-7. PMID:7552746
- ↑ Krusong K, Carpenter EP, Bellamy SR, Savva R, Baldwin GS. A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1. J Biol Chem. 2006 Feb 24;281(8):4983-92. Epub 2005 Nov 22. PMID:16306042 doi:http://dx.doi.org/10.1074/jbc.M509137200
- ↑ Savva R, McAuley-Hecht K, Brown T, Pearl L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature. 1995 Feb 9;373(6514):487-93. PMID:7845459 doi:http://dx.doi.org/10.1038/373487a0
