TY - JOUR
T1 - DNA modification by methyltransferases
AU - Cheng, Xiaodong
N1 - Funding Information:
I am grateful to Richard J Roberts for his encouragement and support; 1 also thank Robert M Blumenthal and Richard J Roberts for critical comments on the manuscript. Work from the author's group was supported in part by a grant from the National Institutes of Health (GM 49245) and the WM Keck Foundation.
PY - 1995/2
Y1 - 1995/2
N2 - Enzymatic methylation of DNA plays important roles in both prokaryotes and eukaryotes. Structural study of the Hhal 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 Hhal 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.
AB - Enzymatic methylation of DNA plays important roles in both prokaryotes and eukaryotes. Structural study of the Hhal 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 Hhal 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.
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U2 - 10.1016/0959-440X(95)80003-J
DO - 10.1016/0959-440X(95)80003-J
M3 - Article
C2 - 7773746
AN - SCOPUS:0028946713
SN - 0959-440X
VL - 5
SP - 4
EP - 10
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 1
ER -