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Significance Type I restriction-modification (R-M) enzymes are large molecular machines found in the majority of bacterial species. They can add methylation modifications to the self-DNA and degrade the invading unmodified DNA. The lack of high-resolution structures of type I R-M complexes impairs our understanding of the mechanism of subunit assembly and conformational transition. Here we report the first high-resolution structure of the type I MTase complex in its “open” conformation, including one DNA-recognition subunit, two DNA-modification subunits, one bound DNA, and two S-adenosyl methionine cofactors. We propose an updated model for the complex assembly and conformational transition. The structural and biochemical characterization of the type I R-M system reported in this study provides guidelines for future applications in molecular biology.

Structural basis underlying complex assembly and conformational transition of the type I R-M system