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Ada metal-binding domain-containing protein
The Escherichia coli Ada protein repairs O6-methylguanine residues and methyl phosphotriesters in DNA by direct transfer of the methyl group to a cysteine residue. This domain contains four conserved cysteines that form a zinc binding site [1,2]. One of these cysteines is a methyl group acceptor. The methylated domain can then specifically bind to the ada box on a DNA duplex [2]. [1]. 1581309. Zinc binding by the methylation signaling domain of the Escherichia coli Ada protein. Myers LC, Terranova MP, Nash HM, Markus MA, Verdine GL;. Biochemistry 1992;31:4541-4547. [2]. 8500619. Folding topology and DNA binding of the N-terminal fragment of Ada protein. Sakashita H, Sakuma T, Ohkubo T, Kainosho M, Sakumi K, Sekiguchi M, Morikawa K;. FEBS Lett 1993;323:252-256. (from Pfam)
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