7CD5

mAPE1-blunt-ended dsDNA product complex

7CD5 の概要

• エントリーDOI: 10.2210/pdb7cd5/pdb
• 分子名称: DNA(5'-D(*CP*GP*TP*AP*AP*TP*AP*CP*G)-3'), DNA-(apurinic or apyrimidinic site) endonuclease (2 entities in total)
• 機能のキーワード: ape1, protein-nucleic acid interaction, exonuclease, dna repair, dna binding protein, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41835.16

構造登録者

Liu, T.C.,Hsiao, Y.Y. (登録日: 2020-06-18, 公開日: 2021-01-13, 最終更新日: 2023-11-29)

主引用文献

Liu, T.C.,Lin, C.T.,Chang, K.C.,Guo, K.W.,Wang, S.,Chu, J.W.,Hsiao, Y.Y.
APE1 distinguishes DNA substrates in exonucleolytic cleavage by induced space-filling.
Nat Commun, 12:601-601, 2021

PubMed Abstract: The exonuclease activity of Apurinic/apyrimidinic endonuclease 1 (APE1) is responsible for processing matched/mismatched terminus in various DNA repair pathways and for removing nucleoside analogs associated with drug resistance. To fill in the gap of structural basis for exonucleolytic cleavage, we determine the APE1-dsDNA complex structures displaying end-binding. As an exonuclease, APE1 does not show base preference but can distinguish dsDNAs with different structural features. Integration with assaying enzyme activity and binding affinity for a variety of substrates reveals for the first time that both endonucleolytic and exonucleolytic cleavage can be understood by an induced space-filling model. Binding dsDNA induces RM (Arg176 and Met269) bridge that defines a long and narrow product pocket for exquisite machinery of substrate selection. Our study paves the way to comprehend end-processing of dsDNA in the cell and the drug resistance relating to APE1.

PubMed: 33504804
DOI: 10.1038/s41467-020-20853-2

実験手法

X-RAY DIFFRACTION (2.7 Å)