Cheng, X. (February 1995) DNA modification by methyltransferases. Curr Opin Struct Biol, 5 (1). pp. 4-10. ISSN 0959-440X (Print)
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.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Amino Acid Sequence Animals DNA/ chemistry/ metabolism Humans Methyltransferases/chemistry/ pharmacology Molecular Sequence Data Nucleic Acid Conformation/ drug effects Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. |
| Subjects: | bioinformatics > genomics and proteomics > design > amino acid design organism description > animal bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase |
| CSHL Authors: | |
| Communities: | CSHL labs |
| Depositing User: | Jessica Koos |
| Date: | February 1995 |
| Date Deposited: | 15 Aug 2014 19:13 |
| Last Modified: | 15 Aug 2014 19:13 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/30573 |
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