8P26

Crystal structure of Arabidopsis thaliana PAXX

8P26 の概要

• エントリーDOI: 10.2210/pdb8p26/pdb
• 分子名称: U2 small nuclear ribonucleoprotein auxiliary factor-like protein (2 entities in total)
• 機能のキーワード: dna repair, non-homologous end joining, scaffold, dna binding protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 263445.31

構造登録者

Ochi, T. (登録日: 2023-05-15, 公開日: 2023-06-28, 最終更新日: 2023-10-04)

主引用文献

Khan, H.,Ochi, T.
Plant PAXX has an XLF-like function and stimulates DNA end joining by the Ku-DNA ligase IV/XRCC4 complex.
Plant J., 116:58-68, 2023

PubMed Abstract: Non-homologous end joining (NHEJ) plays a major role in repairing DNA double-strand breaks and is key to genome stability and editing. The minimal core NHEJ proteins, namely Ku70, Ku80, DNA ligase IV and XRCC4, are conserved, but other factors vary in different eukaryote groups. In plants, the only known NHEJ proteins are the core factors, while the molecular mechanism of plant NHEJ remains unclear. Here, we report a previously unidentified plant ortholog of PAXX, the crystal structure of which showed a similar fold to human 'PAXX'. However, plant PAXX has similar molecular functions to human XLF, by directly interacting with Ku70/80 and XRCC4. This suggests that plant PAXX combines the roles of mammalian PAXX and XLF and that these functions merged into a single protein during evolution. This is consistent with a redundant function of PAXX and XLF in mammals.

PubMed: 37340932
DOI: 10.1111/tpj.16359

実験手法

X-RAY DIFFRACTION (3.6 Å)