Abstract
DNA polymerase X (Pol X) from the African swine fever virus (ASFV) specifically binds intermediates in the single-nucleotide base-excision repair process, an activity indicative of repair function. In addition, Pol X catalyzes DNA polymerization with low nucleotide-insertion fidelity. The structural mechanisms by which DNA polymerases confer high or low fidelity in DNA polymerization remain to be elucidated. The three-dimensional structure of Pol X has been determined. Unlike other DNA polymerases, Pol X is formed from only a palm and a C-terminal subdomain. Pol X has a novel palm subdomain fold, containing a positively charged helix at the DNA binding surface. Purine deoxynucleoside triphosphate (dNTP) substrates bind between the palm and C-terminal subdomain, at a dNTP-binding helix, and induce a unique conformation in Pol X. The purine dNTP–bound conformation and high binding affinity for dGTP–Mg2+ of Pol X may contribute to its low fidelity.
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This research was supported by grants from the National Institutes of Health.
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Maciejewski, M., Shin, R., Pan, B. et al. Solution structure of a viral DNA repair polymerase. Nat Struct Mol Biol 8, 936–941 (2001). https://doi.org/10.1038/nsb1101-936
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DOI: https://doi.org/10.1038/nsb1101-936
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