TY - JOUR
T1 - Universal catalytic domain structure of AdoMet-dependent methyltransferases
AU - Schluckebier, Gerd
AU - O’Gara, Margaret
AU - Saenger, Wolfram
AU - Cheng, Xiaodong
N1 - Funding Information:
This work at Cold Spring Harbor Laboratory was supported by grants from the U.S. National Institutes of Health (GM 49245), the Cold Spring Harbor Association, the W. M. Keck Foundation, and the Robertson Research Fund. The work at Institut fur Kristallographie was supported by the Deutsche Forschungsgemeinschaft through Sonderforschungsbereich 344, the Leibniz-Programm, and the Bundesministerium fur Forschung und Technologie. We thank R. M. Blumenthal for comments on the manuscipt.
PY - 1995/3/17
Y1 - 1995/3/17
N2 - The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyltransferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively. The catalytic domains of the bilobal proteins, M.HhaI and M.TaqI, and the entire single domain of COMT have similar folding with an α/β structure containing a mixed central β-sheet. The functional residues are located in equivalent regions at the carboxyl ends of the parallel β-strands. The cofactor binding sites are almost identical and the essential catalytic amino acids coincide. The comparable protein folding and the existence of equivalent amino acids in similar secondary and tertiary positions indicate that many (if not all) AdoMet-dependent methyltransferases have a common catalytic domain structure. This permits tertiary structure prediction of other DNA, RNA, protein, and small-molecule AdoMet-dependent methyltransferases from their amino acid sequences.
AB - The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyltransferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively. The catalytic domains of the bilobal proteins, M.HhaI and M.TaqI, and the entire single domain of COMT have similar folding with an α/β structure containing a mixed central β-sheet. The functional residues are located in equivalent regions at the carboxyl ends of the parallel β-strands. The cofactor binding sites are almost identical and the essential catalytic amino acids coincide. The comparable protein folding and the existence of equivalent amino acids in similar secondary and tertiary positions indicate that many (if not all) AdoMet-dependent methyltransferases have a common catalytic domain structure. This permits tertiary structure prediction of other DNA, RNA, protein, and small-molecule AdoMet-dependent methyltransferases from their amino acid sequences.
KW - AdoMet-dependent methyltransferases
KW - C-5-methylcytosine
KW - Conserved sequence motifs
KW - N-4-methylcytosine
KW - N-6-methyladenine
KW - Universal catalytic domain structure
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U2 - 10.1006/jmbi.1994.0117
DO - 10.1006/jmbi.1994.0117
M3 - Editorial
C2 - 7897657
AN - SCOPUS:0028956315
SN - 0022-2836
VL - 247
SP - 16
EP - 20
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 1
ER -