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

Publication Type:

Journal Article


Acta Crystallogr Sect F Struct Biol Cryst Commun, Volume 69, Issue Pt 12, p.1328-34 (2013)


Catalytic Domain, Crystallography, X-Ray, Escherichia coli, Gene Expression, Humans, Models, Molecular, Protein Interaction Domains and Motifs, Protein Structure, Secondary, Protein Subunits, Recombinant Proteins, Structural Homology, Protein, Uracil, Uracil-DNA Glycosidase, Vaccinia virus, Viral Proteins


<p>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.</p>