title: DNA modification by methyltransferases.
abstract: Enzymatic methylation of DNA plays important roles in both prokaryotes and eukaryotes. Structural study of the HhaI DNA methyltransferase has provided considerable insight into the chemistry of C5-cytosine methylation. The DNA-protein complex reveals a substrate cytosine flipped out of the double helix during the reaction, and a novel two-loop DNA-binding motif used for both sequence recognition and flipping the base. Structural comparison of HhaI C5-cytosine methyltransferase, TaqI N6-adenine methyltransferase, and catechol O-methyltransferase reveals a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (SAM)-dependent methyltransferases.
authors.affiliation: WM Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, New York 11724, USA.
authors.forename: X
authors.initials: X
authors.lastname: Cheng
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008780:Methyltransferases / Q000737:chemistry / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation / Q000187:drug effects*
chemical_list: D004247:DNA; D008780:Methyltransferases