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.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Conserved Sequence
  • DNA / metabolism
  • DNA-Cytosine Methylases / biosynthesis
  • DNA-Cytosine Methylases / chemistry*
  • Haemophilus / enzymology
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • S-Adenosylmethionine / chemistry*
  • Sequence Homology, Amino Acid
  • X-Ray Diffraction

Substances

  • Recombinant Proteins
  • S-Adenosylmethionine
  • DNA
  • DNA modification methylase HhaI
  • DNA-Cytosine Methylases