1JAJ

Solution Structure of DNA Polymerase X from the African Swine Fever Virus

1JAJ の概要

• エントリーDOI: 10.2210/pdb1jaj/pdb
• NMR情報: BMRB: 5010
• 分子名称: DNA POLYMERASE BETA-LIKE PROTEIN (1 entity in total)
• 機能のキーワード: cis peptide, viral protein
• 由来する生物種: African swine fever virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20351.49

構造登録者

Maciejewski, M.W.,Shin, R.,Pan, B.,Mullen, G.P. (登録日: 2001-05-30, 公開日: 2001-10-31, 最終更新日: 2024-05-01)

主引用文献

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

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: 11685238
DOI: 10.1038/nsb1101-936

実験手法

SOLUTION NMR