1x2i
From Proteopedia
|
Crystal Structure Of Archaeal Xpf/Mus81 Homolog, Hef From Pyrococcus Furiosus, Helix-hairpin-helix Domain
Overview
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.
About this Structure
1X2I is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
Structural and functional analyses of an archaeal XPF/Rad1/Mus81 nuclease: asymmetric DNA binding and cleavage mechanisms., Nishino T, Komori K, Ishino Y, Morikawa K, Structure. 2005 Aug;13(8):1183-92. PMID:16084390
Page seeded by OCA on Sun Nov 25 01:19:13 2007
