Structure-based sequence alignment of three AdoMet-dependent DNA methyltransferases

O'Gara, M., McCloy, K., Malone, T., Cheng, X. (1995) Structure-based sequence alignment of three AdoMet-dependent DNA methyltransferases. Gene, 157 (1-2). pp. 135-8. ISSN 0378-1119 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/7607477
DOI: 10.1016/0378-1119(94)00669-J

Abstract

M.HhaI, M.TaqI and COMT are DNA methyltransferases (MTases) which catalyze the transfer of a methyl group from the cofactor AdoMet to C5 of cytosine, to N6 of adenine and to a hydroxyl group of catechol, respectively. The larger catalytic domains of the bilobal proteins, M.HhaI and M.TaqI, and the entire single domain of COMT have an alpha/beta structure containing a mixed central beta-sheet. These domains have very similar folding. By allowing appropriate 'insertions' or 'deletions' in the backbones of the three structures, it was possible to find more conserved motifs in M.TaqI and COMT. The similarity in protein folding and the equivalence of amino-acid sequences revealed by the structural alignment indicate that many AdoMet-dependent MTases may share a common catalytic domain structure.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Binding Sites Catechol O-Methyltransferase/ chemistry/metabolism Comparative Study Crystallography, X-Ray Molecular Sequence Data Protein Conformation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. S-Adenosylmethionine/ metabolism Sequence Homology, Amino Acid Site-Specific DNA Methyltransferase (Cytosine-Specific)/ chemistry/metabolism Site-Specific DNA-Methyltransferase (Adenine-Specific)/ chemistry/metabolism Structure-Activity Relationship
Subjects: bioinformatics > genomics and proteomics > design > amino acid design
bioinformatics > genomics and proteomics > alignment > sequence alignment
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs
Depositing User: Jessica Koos
Date Deposited: 11 Aug 2014 20:32
Last Modified: 11 Aug 2014 20:32
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30627

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