Structural highlights
Function
UNG_VACCA Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA.
Publication Abstract from PubMed
Poxvirus uracil DNA glycosylases are the most diverse members of the family I uracil DNA glycosylases (UNGs). The crystal structure of the uracil complex of Vaccinia virus uracil DNA glycosylase (D4) was determined at 2.03 A resolution. One uracil molecule was located in the active-site pocket in each of the 12 noncrystallographic symmetry-related D4 subunits. Although the UNGs of the poxviruses (including D4) feature significant differences in the characteristic motifs designated for uracil recognition and in the base-excision mechanism, the architecture of the active-site pocket in D4 is very similar to that in UNGs of other organisms. Overall, the interactions of the bound uracil with the active-site residues are also similar to the interactions previously observed in the structures of human and Escherichia coli UNG.
Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase.,Schormann N, Banerjee S, Ricciardi R, Chattopadhyay D Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1328-34., doi: 10.1107/S1744309113030613. Epub 2013 Nov 28. PMID:24316823[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schormann N, Banerjee S, Ricciardi R, Chattopadhyay D. Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1328-34., doi: 10.1107/S1744309113030613. Epub 2013 Nov 28. PMID:24316823 doi:http://dx.doi.org/10.1107/S1744309113030613
