Cheng, X. D., Kumar, S., Posfai, J., Pflugrath, J. W., Roberts, R. J. (July 1993) Crystal-Structure of the Hhal DNA Methyltransferase Complexed with S-Adenosyl-L-Methionine. Cell, 74 (2). pp. 299-307. ISSN 0092-8674
Abstract
The first three-dimensional structure of a DNA methyltransferase is presented. The crystal structure of the DNA (cytosine-5)-methyltransferase, M.Hhal (recognition sequence: GCGC), complexed with S-adenosyl-L-methionine has been determined and refined at 2.5 angstrom resolution. The core of the structure is dominated by sequence motifs conserved among all DNA (cytosine-5)-methyltransferases, and these are responsible for cofactor binding and methyltransferase function.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | TARGET-RECOGNIZING DOMAINS MACROMOLECULAR CRYSTALLOGRAPHY DETERMINES METHYLATION CATALYTIC MECHANISM ESCHERICHIA-COLI SEQUENCE MOTIFS MET REPRESSOR BINDING PROTEIN EXPRESSION |
| Subjects: | Investigative techniques and equipment > X-Ray Diffraction 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: | July 1993 |
| Date Deposited: | 20 Apr 2016 19:43 |
| Last Modified: | 20 Apr 2016 19:43 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/32492 |
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