Kumar, S., Cheng, X. D., Klimasauskas, S., Mi, S., Posfai, J., Roberts, R. J., Wilson, G. G. (January 1994) The DNA (Cytosine-5) Methyltransferases. Nucleic Acids Research, 22 (1). pp. 1-10. ISSN 0305-1048
Abstract
The m5C-MTases form a closely-knit family of enzymes in which common amino acid sequence motifs almost certainly translate into common structural and functional elements. These common elements are located predominantly in a single structural domain that performs the chemistry of the reaction. Sequence-specific DNA recognition is accomplished by a separate domain that contains recognition elements not seen in other structures. This, combined with the novel and unexpected mechanistic feature of trapping a base out of the DNA helix, makes the m5C-MTases an intriguing class of enzymes for further study. The reaction pathway has suddenly become more complicated because of the base-flipping and much remains to be learned about the DNA recognition elements in the family members for which structural information is not yet available.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | RESTRICTION-MODIFICATION SYSTEM TARGET-RECOGNIZING DOMAINS BACILLUS-SUBTILIS PHAGES AMINO-ACID-SEQUENCE NUCLEOTIDE-SEQUENCE MODIFICATION METHYLASE NEISSERIA-GONORRHOEAE MODIFICATION GENES ESCHERICHIA-COLI MOLECULAR CHARACTERIZATION |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase |
| CSHL Authors: | |
| Communities: | CSHL labs > Roberts lab |
| Depositing User: | Matt Covey |
| Date: | January 1994 |
| Date Deposited: | 08 May 2015 14:40 |
| Last Modified: | 08 May 2015 14:40 |
| PMCID: | PMC307737 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/31458 |
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