Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine.
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.
Cheng
X
X
W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, New York 11724.
Kumar
S
S
Posfai
J
J
Pflugrath
J W
JW
Roberts
R J
RJ
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D004247:DNA / Q000378:metabolism; D015257:DNA-Cytosine Methylases / Q000096:biosynthesis / Q000737:chemistry*; D006190:Haemophilus / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D012436:S-Adenosylmethionine / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D012436:S-Adenosylmethionine; D004247:DNA; C037664:DNA modification methylase HhaI; D015257:DNA-Cytosine Methylases