1X2I

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

Summary for 1X2I

• Entry DOI: 10.2210/pdb1x2i/pdb
• Related: 1J22 1J23 1J24 1J25 1WP9
• Descriptor: Hef helicase/nuclease (2 entities in total)
• Functional Keywords: alpha helix, helix-hairpin-helix dna binding domain, homodimer, hydrolase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 2
• Total formula weight: 16975.91

Authors

Nishino, T.,Komori, K.,Ishino, Y.,Morikawa, K. (deposition date: 2005-04-24, release date: 2005-09-13, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.45 Å)