Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine

  • Cell. 1993 Jul 30;74(2):299-307. doi: 10.1016/0092-8674(93)90421-l.
X Cheng  1 ,  S Kumar ,  J Posfai ,  J W Pflugrath ,  R J Roberts
Affiliations
  • 1. W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, New York 11724.
PMID: 8343957 DOI: 10.1016/0092-8674(93)90421-l
Abstract

The first three-dimensional structure of a DNA Methyltransferase is presented. The crystal structure of the DNA (cytosine-5)-methyltransferase, M.HhaI (recognition sequence: GCGC), complexed with S-adenosyl-L-methionine has been determined and refined at 2.5 A resolution. The core of the structure is dominated by sequence motifs conserved among all DNA (cytosine-5)-methyltransferases, and these are responsible for cofactor binding and methyltransferase function.

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