2fok

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spinqualitylabelsall models 2fok, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 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

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