| Restriction endonuclease Fok1, C terminal | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| Symbol | Endonuc-Fok1_C | ||||||||
| Pfam | PF09254 | ||||||||
| Pfam clan | CL0415 | ||||||||
| InterPro | IPR015334 | ||||||||
| SCOP2 | 2fok / SCOPe / SUPFAM | ||||||||
| |||||||||
The restriction endonuclease Fok1, naturally found in Flavobacterium okeanokoites, is a bacterial type IIS restriction endonuclease consisting of an N-terminal DNA-binding domain and a non sequence-specific DNA cleavage domain at the C-terminal.[2] Once the protein is bound to duplex DNA via its DNA-binding domain at the 5'-GGATG-3' recognition site, the DNA cleavage domain is activated and cleaves the DNA at two locations, regardless of the nucleotide sequence at the cut site. The DNA is cut 9 nucleotides downstream of the motif on the forward strand, and 13 nucleotides downstream of the motif on the reverse strand,[3] producing two sticky ends with 4-bp overhangs.
Its molecular mass is 65.4 kDa, being composed of 587 amino acids.
- ^ Aggarwal, A. K.; Wah, D. A.; Hirsch, J. A.; Dorner, L. F.; Schildkraut, I. (1997). "Structure of the multimodular endonuclease Fok1 bound to DNA". Nature. 388 (6637): 97–100. doi:10.1038/40446. PMID 9214510. S2CID 205027830.
- ^ Durai S, Mani M, Kandavelou K, Wu J, Porteus M, Chandrasegaran S (2005). "Zinc finger nucleases: custom-designed molecular scissors for genome engineering of plant and mammalian cells". Nucleic Acids Res. 33 (18): 5978–90. doi:10.1093/nar/gki912. PMC 1270952. PMID 16251401.
- ^ Wah, D. A.; Bitinaite, J.; Schildkraut, I.; Aggarwal, A. K. (1998). "Structure of Fok1 has implications for DNA cleavage". Proc Natl Acad Sci USA. 95 (18): 10564–9. Bibcode:1998PNAS...9510564W. doi:10.1073/pnas.95.18.10564. PMC 27934. PMID 9724743.