1J22: Crystal Structure Of Archaeal XpfMUS81 HOMOLOG, HEF FROM PYROCOCCUS Furiosus, Nuclease Domain, Selenomet Derivative

The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. Here, we report the domain organization of an archaeal homolog (Hef) of this family and the X-ray crystal structure of the middle domain, with the nuclease activity. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases, including the correspondence of the GDX(n)ERKX(3)D signature motif in Hef to the PDX(n)(E/D)XK motif in restriction enzymes. This structural study also suggests that the XPF/Rad1/Mus81/ERCC1 proteins form a dimer through each interface of the nuclease domain and the helix-hairpin-helix domain. Simultaneous disruptions of both interfaces result in their dissociation into separate monomers, with strikingly reduced endonuclease activities.
PDB ID: 1J22Download
MMDB ID: 22568
PDB Deposition Date: 2002/12/25
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 1J22: dimeric; determined by author
Molecular Components in 1J22
Label Count Molecule
Proteins (2 molecules)
Atp-dependent RNA Helicase, Putative
Molecule annotation
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Citing MMDB