Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase.

@article{Horton2006StructureAS,
  title={Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase.},
  author={John R. Horton and Kirsten Liebert and Mikl{\'o}s B{\'e}k{\'e}s and Albert Jeltsch and Xiaodong Cheng},
  journal={Journal of molecular biology},
  year={2006},
  volume={358 2},
  pages={559-70}
}
The structure of the Escherichia coli Dam DNA-(adenine-N6)-methyltransferase in complex with cognate DNA was determined at 1.89 A resolution in the presence of S-adenosyl-L-homocysteine. DNA recognition and the dynamics of base-flipping were studied by site-directed mutagenesis, DNA methylation kinetics and fluorescence stopped-flow experiments. Our data illustrate the mechanism of coupling of DNA recognition and base-flipping. Contacts to the non-target strand in the second (3') half of the… CONTINUE READING