Enzyme-promoted base flipping controls DNA methylation fidelity.

@article{Matje2013EnzymepromotedBF,
  title={Enzyme-promoted base flipping controls DNA methylation fidelity.},
  author={Douglas M Matje and Hongjun Zhou and D Alastair M Smith and Robert K Neely and David T. F. Dryden and Anita C. Jones and Frederick W. Dahlquist and Norbert O Reich},
  journal={Biochemistry},
  year={2013},
  volume={52 10},
  pages={1677-85}
}
A quantitative understanding of how conformational transitions contribute to enzyme catalysis and specificity remains a fundamental challenge. A suite of biophysical approaches was used to reveal several transient states of the enzyme-substrate complexes of the model DNA cytosine methyltransferase M.HhaI. Multidimensional, transverse relaxation-optimized nuclear magnetic resonance (NMR) experiments show that M.HhaI has the same conformation with noncognate and cognate DNA sequences. The high… CONTINUE READING