1X2I

Crystal Structure Of Archaeal Xpf/Mus81 Homolog, Hef From Pyrococcus Furiosus, Helix-hairpin-helix Domain

1X2I の概要

• エントリーDOI: 10.2210/pdb1x2i/pdb
• 関連するPDBエントリー: 1J22 1J23 1J24 1J25 1WP9
• 分子名称: Hef helicase/nuclease (2 entities in total)
• 機能のキーワード: alpha helix, helix-hairpin-helix dna binding domain, homodimer, hydrolase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16975.91

構造登録者

Nishino, T.,Komori, K.,Ishino, Y.,Morikawa, K. (登録日: 2005-04-24, 公開日: 2005-09-13, 最終更新日: 2024-03-13)

主引用文献

Nishino, T.,Komori, K.,Ishino, Y.,Morikawa, K.
Structural and Functional Analyses of an Archaeal XPF/Rad1/Mus81 Nuclease: Asymmetric DNA Binding and Cleavage Mechanisms
STRUCTURE, 13:1183-1192, 2005

PubMed Abstract: XPF/Rad1/Mus81/Hef proteins recognize and cleave branched DNA structures. XPF and Rad1 proteins cleave the 5' side of nucleotide excision repair bubble, while Mus81 and Hef cleave similar sites of the nicked Holliday junction, fork, or flap structure. These proteins all function as dimers and consist of catalytic and helix-hairpin-helix DNA binding (HhH) domains. We have determined the crystal structure of the HhH domain of Pyrococcus furiosus Hef nuclease (HefHhH), which revealed the distinct mode of protein dimerization. Our structural and biochemical analyses also showed that each of the catalytic and HhH domains binds to distinct regions within the fork-structured DNA: each HhH domain from two separate subunits asymmetrically binds to the arm region, while the catalytic domain binds near the junction center. Upon binding to DNA, Hef nuclease disrupts base pairs near the cleavage site. It is most likely that this bipartite binding mode is conserved in the XPF/Rad1/Mus81 nuclease family.

PubMed: 16084390
DOI: 10.1016/j.str.2005.04.024

実験手法

X-RAY DIFFRACTION (1.45 Å)