1J24

Crystal structure of archaeal XPF/Mus81 homolog, Hef from Pyrococcus furiosus, nuclease domain, Ca cocrystal

Summary for 1J24

• Entry DOI: 10.2210/pdb1j24/pdb
• Related: 1J22 1J23 1J25
• Descriptor: ATP-dependent RNA helicase, putative, CALCIUM ION (3 entities in total)
• Functional Keywords: structure-specific endonuclease, hydrolase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 16156.74

Authors

Nishino, T.,Komori, K.,Ishino, Y.,Morikawa, K. (deposition date: 2002-12-25, release date: 2003-04-22, Last modification date: 2024-04-03)

Primary citation

Nishino, T.,Komori, K.,Ishino, Y.,Morikawa, K.
X-Ray and Biochemical Anatomy of an Archaeal XPF/Rad1/Mus81 Family Nuclease. Similarity between Its Endonuclease Domain and Restriction Enzymes
Structure, 11:445-457, 2003

PubMed Abstract: 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.

PubMed: 12679022
DOI: 10.1016/S0969-2126(03)00046-7

Experimental method

X-RAY DIFFRACTION (1.78 Å)