7AEO

Human ARTD2 in complex with DNA oligonucleotides

7AEO の概要

• エントリーDOI: 10.2210/pdb7aeo/pdb
• 分子名称: Poly [ADP-ribose] polymerase 2, DNA, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: artd2, parp2, dna-damage, dna-repair, adp-ribosylation, dna-binding protein, dna binding protein
• 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: 66713.29

構造登録者

Obaji, E.,Maksimainen, M.M.,Galera-Prat, A.,Lehtio, L. (登録日: 2020-09-17, 公開日: 2021-05-19, 最終更新日: 2024-01-31)

主引用文献

Obaji, E.,Maksimainen, M.M.,Galera-Prat, A.,Lehtio, L.
Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition.
Nat Commun, 12:3479-3479, 2021

PubMed Abstract: Human PARP2/ARTD2 is an ADP-ribosyltransferase which, when activated by 5'-phosphorylated DNA ends, catalyses poly-ADP-ribosylation of itself, other proteins and DNA. In this study, a crystal structure of PARP2 in complex with an activating 5'-phosphorylated DNA shows that the WGR domain bridges the dsDNA gap and joins the DNA ends. This DNA binding results in major conformational changes, including reorganization of helical fragments, in the PARP2 regulatory domain. A comparison of PARP1 and PARP2 crystal structures reveals how binding to a DNA damage site leads to formation of a catalytically competent conformation. In this conformation, PARP2 is capable of binding substrate NAD and histone PARylation factor 1 that changes PARP2 residue specificity from glutamate to serine when initiating DNA repair processes. The structure also reveals how the conformational changes in the autoinhibitory regulatory domain would promote the flexibility needed by the enzyme to reach the target macromolecule for ADP-ribosylation.

PubMed: 34108479
DOI: 10.1038/s41467-021-23800-x

実験手法

X-RAY DIFFRACTION (2.8 Å)