The DNA (cytosine-5) methyltransferases.
The m5C-MTases form a closely-knit family of enzymes in which common amino acid sequence motifs almost certainly translate into common structural and functional elements. These common elements are located predominantly in a single structural domain that performs the chemistry of the reaction. Sequence-specific DNA recognition is accomplished by a separate domain that contains recognition elements not seen in other structures. This, combined with the novel and unexpected mechanistic feature of trapping a base out of the DNA helix, makes the m5C-MTases an intriguing class of enzymes for further study. The reaction pathway has suddenly become more complicated because of the base-flipping and much remains to be learned about the DNA recognition elements in the family members for which structural information is not yet available.
Kumar
S
S
New England Biolabs, Beverly, MA 01915.
Cheng
X
X
Klimasauskas
S
S
Mi
S
S
Posfai
J
J
Roberts
R J
RJ
Wilson
G G
GG
D000595:Amino Acid Sequence; D015257:DNA-Cytosine Methylases / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012436:S-Adenosylmethionine / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D012436:S-Adenosylmethionine; D015257:DNA-Cytosine Methylases