FokI Restriction Endonuclease; Chain A, domain 1
Nucleotide sequence of the FokI restriction-modification system: separate strand-specificity domains in the methyltransferase.
Functional domains in Fok I restriction endonuclease.
Alteration of the cleavage distance of Fok I restriction endonuclease by insertion mutagenesis.
Single amino acid substitutions uncouple the DNA binding and strand scission activities of Fok I endonuclease.
Insertion and deletion mutants of FokI restriction endonuclease.
Crystallization and preliminary X-ray analysis of restriction endonuclease FokI bound to DNA.
Site-specific cleavage of DNA-RNA hybrids by zinc finger/FokI cleavage domain fusions.
Structure of the multimodular endonuclease FokI bound to DNA.
Chimeric restriction enzyme: Gal4 fusion to FokI cleavage domain.
The mechanism of DNA cleavage by the type II restriction enzyme EcoRV: Asp36 is not directly involved in DNA cleavage but serves to couple indirect readout to catalysis.
FokI dimerization is required for DNA cleavage.
Structure of FokI has implications for DNA cleavage.
Type II restriction endonucleases: structural, functional and evolutionary relationships.
A detailed study of the substrate specificity of a chimeric restriction enzyme.
Identification of the metal-binding sites of restriction endonucleases by Fe2+-mediated oxidative cleavage.
Phylogeny of the restriction endonuclease-like superfamily inferred from comparison of protein structures.
Requirements for double-strand cleavage by chimeric restriction enzymes with zinc finger DNA-recognition domains.
Substrate-assisted catalysis: molecular basis and biological significance.
FokI requires two specific DNA sites for cleavage.
Stimulation of homologous recombination through targeted cleavage by chimeric nucleases.
Many type IIs restriction endonucleases interact with two recognition sites before cleaving DNA.
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
In vitro selection of restriction endonucleases by in vitro compartmentalization.
Although the detailed mechanism of the reaction has not been elucidated, the catalytic site is similar to the other Type II restriction enzymes, such as EcoRV (S00403 in EzCatDB) and BglI (S00405 in EzCatDB). Thus, the catalytic mechanism of this enzyme might be similar to that of those enzymes. More recent paper [20] supported the substrate-assisted mechanism for the related enzymes (type II restriction enzymes), ruling out the two-metal-ion mechanism. Thus, we concluded that this enzyme adopts the substrate-assisted mechanism with only one metal ion for catalysis (see EcoRV; S00404 in EzCatDB).