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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Solution structure of a viral DNA repair polymerase.

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-Mg(2+) of Pol X may contribute to its low fidelity.[1]

References

  1. Solution structure of a viral DNA repair polymerase. Maciejewski, M.W., Shin, R., Pan, B., Marintchev, A., Denninger, A., Mullen, M.A., Chen, K., Gryk, M.R., Mullen, G.P. Nat. Struct. Biol. (2001) [Pubmed]
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