J. Labahn et al., 3-DIMENSIONAL STRUCTURE OF THE ADENINE-SPECIFIC DNA METHYLTRANSFERASEM-CENTER-DOT-TAQ-I IN COMPLEX WITH THE COFACTOR S-ADENOSYLMETHIONINE, Proceedings of the National Academy of Sciences of the United Statesof America, 91(23), 1994, pp. 10957-10961
The Thermus aquaticus DNA methyltransferase M.Taq I (EC 2.1.1.72) meth
ylates N-6 of adenine in the specific double-helical DNA sequence TCGA
by transfer of -CH3 from the cofactor S-adenosyl-L-methionine. The x-
ray crystal structure at 2.4-Angstrom resolution of this enzyme in com
plex with S-adenosylmethionine shows alpha/beta folding of the polypep
tide into two domains of about equal size. They are arranged in the fo
rm of a C with a wide deft suitable to accommodate the DNA substrate.
The N-terminal domain is dominated by a nine-stranded beta-sheet; it c
ontains the two observed segments typical for N-methyltransferases whi
ch form a pocket for cofactor binding. The C-terminal domain is formed
by four small beta-sheets and alpha helices. The three-dimensional fo
lding of M.Taq I is similar to that of the cytosine-specific Hha I met
hyltransferase, where the large beta-sheet in the N-terminal domain co
ntains all conserved segments and the enzymatically functional parts,
and the smaller C-terminal domain is less structured.