Structure of the multimodular endonuclease FokI bound to DNA

@article{Wah1997StructureOT,
  title={Structure of the multimodular endonuclease FokI bound to DNA},
  author={David A. Wah and Joel A. Hirsch and Lydia F. Dorner and Ira Schildkraut and Aneel K. Aggarwal},
  journal={Nature},
  year={1997},
  volume={388},
  pages={97-100}
}
FokI is a member of an unusual class of bipartite restriction enzymes that recognize a specific DNA sequence and cleave DNA nonspecifically a short distance away from that sequence. Because of its unusual bipartite nature, FokI has been used to create artificial enzymes with new specificities. We have determined the crystal structure at 2.8 Å resolution of the complete FokI enzyme bound to DNA. As anticipated, the enzyme contains amino- and carboxy-terminal domains corresponding to the DNA… 
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  • 1998
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The results identify the DNA-binding domain, imply that DNA cleavage and recognition are independent and separable, and lead us to speculate about a cleft-like structure for NaeI.
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A model is proposed that requires the dimerization of FokI on DNA to cleave both DNA strands and is corroboration with the cleavage data presented in the accompanying paper.
Protein assembly and DNA looping by the FokI restriction endonuclease
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The BglI–DNA complex demonstrates, for the first time, that a conserved subunit fold can dimerize in more than one way, resulting in different DNA cleavage patterns.
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TLDR
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TLDR
Type II restriction endonucleases recognize short, usually palindromic, sequences of 4-8 bp and, in the presence of Mg(2+), cleave the DNA within or in close proximity to the recognition sequence.
Characterization and crystal structure of the type IIG restriction endonuclease RM.BpuSI
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Targeting individual subunits of the FokI restriction endonuclease to specific DNA strands
Many restriction endonucleases are dimers that act symmetrically at palindromic DNA sequences, with each active site cutting one strand. In contrast, FokI acts asymmetrically at a non-palindromic
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