Abstract
The first three-dimensional structure of a DNA methyltransferase is presented. The crystal structure of the DNA (cytosine-5)-methyltransferase, M.HhaI (recognition sequence: GCGC), complexed with S-adenosyl-L-methionine has been determined and refined at 2.5 A 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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Conserved Sequence
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DNA / metabolism
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DNA-Cytosine Methylases / biosynthesis
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DNA-Cytosine Methylases / chemistry*
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Haemophilus / enzymology
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Models, Molecular
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Molecular Sequence Data
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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S-Adenosylmethionine / chemistry*
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Sequence Homology, Amino Acid
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X-Ray Diffraction
Substances
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Recombinant Proteins
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S-Adenosylmethionine
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DNA
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DNA modification methylase HhaI
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DNA-Cytosine Methylases