Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly.

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.

Results

Results of dynamic light scattering experiments and native size exclusion chromatogra

SUBMITTER: Schormann N 

PROVIDER: S-EPMC1936997 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature