PMID:9383376
| Citation |
Myers, LC, Cushing, TD, Wagner, G and Verdine, GL (1994) Metal-coordination sphere in the methylated Ada protein-DNA co-complex. Chem. Biol. 1:91-7 |
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| Abstract |
The Ada protein of Escherichia coli repairs methyl phosphotriesters in DNA by direct, irreversible methyl transfer to one of its own cysteine residues. This residue, Cys69, is ligated to a tightly bound zinc ion in the protein. After methyl transfer, Ada can bind DNA sequence-specifically, inducing the transcription of genes that confer resistance to the toxic effects of methylating agents. Coordination of zinc via a thioether-S is exceedingly rare. We therefore investigated whether methylation causes ligand exchange of Cys69, replacing the thioether with a new zinc ligand with higher affinity for the metal. |
| Links | |
| Keywords |
Bacterial Proteins/biosynthesis; Bacterial Proteins/chemistry; DNA Methylation; DNA, Bacterial/biosynthesis; DNA, Bacterial/chemistry; Escherichia coli Proteins; Metals/chemistry; O(6)-Methylguanine-DNA Methyltransferase; Transcription Factors; Zinc/chemistry |
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