Crystal-Structure of the Hhal DNA Methyltransferase Complexed with S-Adenosyl-L-Methionine

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

URL: http://www.ncbi.nlm.nih.gov/pubmed/8343957
DOI: 10.1016/0092-8674(93)90421-L

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: http://repository.cshl.edu/id/eprint/32492

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving