2fok
From Proteopedia
STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI
Overview
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.
About this Structure
2FOK is a Single protein structure of sequence from Planomicrobium okeanokoites. Full crystallographic information is available from OCA.
Reference
Structure of FokI has implications for DNA cleavage., Wah DA, Bitinaite J, Schildkraut I, Aggarwal AK, Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10564-9. PMID:9724743 Page seeded by OCA on Sun May 4 04:08:20 2008
Categories: Planomicrobium okeanokoites | Single protein | Type II site-specific deoxyribonuclease | Aggarwal, A K. | Bitinaite, J. | Schildkraut, I. | Wah, D A. | Deoxyribonuclease | Dna cleavage | Dna hydrolysis | Dna-binding protein | Metal ion catalysis | Metalloenzyme | Nucleic acid recognition | Type iis restriction endonuclease
