Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase

نویسندگان

  • N. Schormann
  • S. Banerjee
  • R. Ricciardi
  • D. Chattopadhyay
چکیده

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.

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عنوان ژورنال:

دوره 69  شماره 

صفحات  -

تاریخ انتشار 2013