2ZJ8
Archaeal DNA helicase Hjm apo state in form 2
Summary for 2ZJ8
Entry DOI | 10.2210/pdb2zj8/pdb |
Related | 2ZJ2 2ZJ5 2ZJA |
Descriptor | Putative ski2-type helicase (2 entities in total) |
Functional Keywords | reca fold, atp-binding, helicase, hydrolase, nucleotide-binding |
Biological source | Pyrococcus furiosus |
Total number of polymer chains | 1 |
Total formula weight | 82746.40 |
Authors | Oyama, T.,Oka, H.,Fujikane, R.,Ishino, Y.,Morikawa, K. (deposition date: 2008-02-29, release date: 2009-02-10, Last modification date: 2023-11-01) |
Primary citation | Oyama, T.,Oka, H.,Mayanagi, K.,Shirai, T.,Matoba, K.,Fujikane, R.,Ishino, Y.,Morikawa, K. Atomic structures and functional implications of the archaeal RecQ-like helicase Hjm Bmc Struct.Biol., 9:2-2, 2009 Cited by PubMed Abstract: Pyrococcus furiosus Hjm (PfuHjm) is a structure-specific DNA helicase that was originally identified by in vitro screening for Holliday junction migration activity. It belongs to helicase superfamily 2, and shares homology with the human DNA polymerase Theta (PolTheta), HEL308, and Drosophila Mus308 proteins, which are involved in DNA repair. Previous biochemical and genetic analyses revealed that PfuHjm preferentially binds to fork-related Y-structured DNAs and unwinds their double-stranded regions, suggesting that this helicase is a functional counterpart of the bacterial RecQ helicase, which is essential for genome maintenance. Elucidation of the DNA unwinding and translocation mechanisms by PfuHjm will require its three-dimensional structure at atomic resolution. PubMed: 19159486DOI: 10.1186/1472-6807-9-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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