2FOK

STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI

Summary for 2FOK

• Entry DOI: 10.2210/pdb2fok/pdb
• Descriptor: FOKI RESTRICTION ENDONUCLEASE (2 entities in total)
• Functional Keywords: nucleic acid recognition, dna-binding protein, type iis restriction endonuclease, deoxyribonuclease, dna hydrolysis, dna cleavage, metalloenzyme, metal ion catalysis
• Biological source: Planomicrobium okeanokoites
• Total number of polymer chains: 2
• Total formula weight: 131667.25

Authors

Wah, D.A.,Bitinaite, J.,Schildkraut, I.,Aggarwal, A.K. (deposition date: 1998-03-30, release date: 1998-06-17, Last modification date: 2024-05-29)

Primary citation

Wah, D.A.,Bitinaite, J.,Schildkraut, I.,Aggarwal, A.K.
Structure of FokI has implications for DNA cleavage.
Proc.Natl.Acad.Sci.Usa, 95:10564-10569, 1998

PubMed Abstract: FokI is a member an unusual class of restriction enzymes that recognize a specific DNA sequence and cleave nonspecifically a short distance away from that sequence. FokI consists of an N-terminal DNA recognition domain and a C-terminal cleavage domain. The bipartite nature of FokI has led to the development of artificial enzymes with novel specificities. We have solved the structure of FokI to 2.3 A resolution. The structure reveals a dimer, in which the dimerization interface is mediated by the cleavage domain. Each monomer has an overall conformation similar to that found in the FokI-DNA complex, with the cleavage domain packing alongside the DNA recognition domain. In corroboration with the cleavage data presented in the accompanying paper in this issue of Proceedings, we propose a model for FokI DNA cleavage that requires the dimerization of FokI on DNA to cleave both DNA strands.

PubMed: 9724743
DOI: 10.1073/pnas.95.18.10564

Experimental method

X-RAY DIFFRACTION (2.3 Å)