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Structure of FokI has implications for DNA cleavage.

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.

SUBMITTER: Wah DA

PROVIDER: S-EPMC27934 | biostudies-literature | 1998 Sep

REPOSITORIES: biostudies-literature

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Structure of FokI has implications for DNA cleavage.

Wah D A DA Bitinaite J J Schildkraut I I Aggarwal A K AK

Proceedings of the National Academy of Sciences of the United States of America 19980901 18

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 ...[more]

PMID: 9724743

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Project description:This SuperSeries is composed of the SubSeries listed below.

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