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• W2136668031 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." @default.
• W2136668031 created "2016-06-24" @default.
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• W2136668031 date "2013-11-28" @default.
• W2136668031 modified "2023-09-27" @default.
• W2136668031 title "Structure of the uracil complex of<i>Vaccinia virus</i>uracil DNA glycosylase" @default.
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• W2136668031 doi "https://doi.org/10.1107/s1744309113030613" @default.
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