1JAJ
Solution Structure of DNA Polymerase X from the African Swine Fever Virus
Summary for 1JAJ
| Entry DOI | 10.2210/pdb1jaj/pdb |
| NMR Information | BMRB: 5010 |
| Descriptor | DNA POLYMERASE BETA-LIKE PROTEIN (1 entity in total) |
| Functional Keywords | cis peptide, viral protein |
| Biological source | African swine fever virus |
| Total number of polymer chains | 1 |
| Total formula weight | 20351.49 |
| Authors | Maciejewski, M.W.,Shin, R.,Pan, B.,Mullen, G.P. (deposition date: 2001-05-30, release date: 2001-10-31, Last modification date: 2024-05-01) |
| Primary citation | Maciejewski, M.W.,Shin, R.,Pan, B.,Marintchev, A.,Denninger, A. Solution structure of a viral DNA repair polymerase. Nat.Struct.Biol., 8:936-941, 2001 Cited by PubMed 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-Mg(2+) of Pol X may contribute to its low fidelity. PubMed: 11685238DOI: 10.1038/nsb1101-936 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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