6W0R

Human 8-oxoguanine glycosylase interrogating fully intrahelical undamaged DNA

6W0R の概要

• エントリーDOI: 10.2210/pdb6w0r/pdb
• 分子名称: N-glycosylase/DNA lyase, DNA (5'-D(P*CP*AP*GP*GP*TP*C)-3'), DNA (5'-D(P*CP*CP*TP*GP*G)-3'), ... (7 entities in total)
• 機能のキーワード: hogg1, 8-oxog, encounter complex, interrogation complex, dna binding protein, lyase-dna complex, lyase/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 38966.44

構造登録者

Shigdel, U.,Verdine, G. (登録日: 2020-03-02, 公開日: 2020-09-23, 最終更新日: 2024-11-13)

主引用文献

Shigdel, U.K.,Ovchinnikov, V.,Lee, S.J.,Shih, J.A.,Karplus, M.,Nam, K.,Verdine, G.L.
The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase.
Nat Commun, 11:4437-4437, 2020

PubMed Abstract: Efficient search for DNA damage embedded in vast expanses of the DNA genome presents one of the greatest challenges to DNA repair enzymes. We report here crystal structures of human 8-oxoguanine (oxoG) DNA glycosylase, hOGG1, that interact with the DNA containing the damaged base oxoG and the normal base G while they are nested in the DNA helical stack. The structures reveal that hOGG1 engages the DNA using different protein-DNA contacts from those observed in the previously determined lesion recognition complex and other hOGG1-DNA complexes. By applying molecular dynamics simulations, we have determined the pathways taken by the lesion and normal bases when extruded from the DNA helix and their associated free energy profiles. These results reveal how the human oxoG DNA glycosylase hOGG1 locates the lesions inside the DNA helix and facilitates their extrusion for repair.

PubMed: 32895378
DOI: 10.1038/s41467-020-18290-2

実験手法

X-RAY DIFFRACTION (2.35 Å)