Type I restriction-modification enzymes act as conventional adenine methylases on hemimethylated DNAs, but unmethylated recognition targets induce them to translocate thousands of base pairs before cleaving distant sites nonspecifically. The first crystal structure of a type I motor subunit responsible for translocation and cleavage suggests how the pentameric translocating complex is assembled and provides a structural framework for translocation of duplex DNA by RecA-like ATPase motors.

Department of Structure and Function of Proteins Institute of Systems Biology and Ecology Academy of Sciences of the Czech Republic Nove Hrady Czech Republic

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Crystal structure of a novel domain of the motor subunit of the Type I restriction enzyme EcoR124 involved in complex assembly and DNA binding

A residue of motif III positions the helicase domains of motor subunit HsdR in restriction-modification enzyme EcoR124I

The helical domain of the EcoR124I motor subunit participates in ATPase activity and dsDNA translocation

pHluorin-assisted expression, purification, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I

Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme

Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I

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PDB
2W00