1g60

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Revision as of 13:36, 20 November 2007

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spinqualitylabelsall models 1g60, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Methyltransferase MboIIa (Moraxella bovis)

Overview

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 A resolution the crystal structure of, a beta-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.

About this Structure

1G60 is a Single protein structure of sequence from Moraxella bovis with NA and SAM as ligands. Active as Site-specific DNA-methyltransferase (adenine-specific), with EC number 2.1.1.72 Full crystallographic information is available from OCA.

Reference

Crystal structure of MboIIA methyltransferase., Osipiuk J, Walsh MA, Joachimiak A, Nucleic Acids Res. 2003 Sep 15;31(18):5440-8. PMID:12954781

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