Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly |
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| Authors: | Norbert Schormann Alexei Grigorian Alexandra Samal Raman Krishnan Lawrence DeLucas Debasish Chattopadhyay |
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| Institution: | (1) Center for Biophysical Sciences & Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA;(2) BioCryst Pharmaceuticals, Birmingham, AL 35244, USA;(3) Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA |
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| Abstract: | Background Uracil-DNA glycosylases (UDGs) catalyze excision of uracil from DNA. Vaccinia virus, which is the prototype of poxviruses,
encodes a UDG (vvUDG) that is significantly different from the UDGs of other organisms in primary, secondary and tertiary
structure and characteristic motifs. It adopted a novel catalysis-independent role in DNA replication that involves interaction
with a viral protein, A20, to form the processivity factor. UDG:A20 association is essential for assembling of the processive
DNA polymerase complex. The structure of the protein must have provisions for such interactions with A20. This paper provides
the first glimpse into the structure of a poxvirus UDG. |
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