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Nucleic Acids Research, 2003, Vol. 31, No. 18 5440-5448
© 2003 Oxford University Press

Crystal structure of MboIIA methyltransferase

Jerzy Osipiuk1,2, Martin A. Walsh3 and Andrzej Joachimiak*,1

1 Argonne National Laboratory, Biosciences Division and Structural Biology Center, 9700 South Cass Avenue, Argonne, IL 60439, USA, 2 University of Gdansk, Department of Microbiology, Kladki 24, 80-822 Gdansk, Poland and 3 Medical Research Council France, c/o ESRF, F-38043 Grenoble Cedex, France

*To whom correspondence should be addressed. Tel: +1 630 252 3926; Fax: +1 630 252 6126; Email: andrzejj{at}anl.gov

DNA methyltransferases (MTases) are sequence-specific enzymes which transfer a methyl group from S-adenosyl-L-methionine (AdoMet) to the amino group of either cytosine or adenine within a recognized DNA sequence. Methylation of a base in a specific DNA sequence protects DNA from nucleolytic cleavage by restriction enzymes recognizing the same DNA sequence. We have determined at 1.74 Å resolution the crystal structure of a ß-class DNA MTase MboIIA (M·MboIIA) from the bacterium Moraxella bovis, the smallest DNA MTase determined to date. M·MboIIA methylates the 3' adenine of the pentanucleotide sequence 5'-GAAGA-3'. The protein crystallizes with two molecules in the asymmetric unit which we propose to resemble the dimer when M·MboIIA is not bound to DNA. The overall structure of the enzyme closely resembles that of M·RsrI. However, the cofactor-binding pocket in M·MboIIA forms a closed structure which is in contrast to the open-form structures of other known MTases.


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