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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1328-34. doi: 10.1107/S1744309113030613. Epub 2013 Nov 28.

Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase.

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1
Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Abstract

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 Å 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.

KEYWORDS:

Vaccinia virus; uracil DNA glycosidase

PMID:
24316823
PMCID:
PMC3855713
DOI:
10.1107/S1744309113030613
[Indexed for MEDLINE]
Free PMC Article
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