PMID:12509243
| Citation |
Bujnicki, JM and Rychlewski, L (2002) Fold-recognition analysis predicts that the Tag protein family shares a common domain with the helix-hairpin-helix DNA glycosylases. DNA Repair (Amst.) 1:391-5 |
|---|---|
| Abstract |
The Escherichia coli protein Tag is traditionally regarded as an archetype of one of four classes of N-alkylpurine DNA glycosylases. However, its structure and phylogenetic relationship to other glycosylases remains a mystery. Fold-recognition and sequence profile analyses suggest that Tag shares the catalytic domain with helix-hairpin-helix (HhH) glycosylases such as MutY, AlkA and EndoIII, but its N- and C-termini together form a unique His2Cys2 cluster. The findings presented in this paper provide insight into sequence-structure-function relationships in the Tag family and should aid in a more precise definition of the common core of the HhH superfamily of glycosylases involved in DNA repair. |
| Links | |
| Keywords |
Amino Acid Sequence; Antigens; Computational Biology; DNA Glycosylases; DNA Repair; Deoxyribonuclease (Pyrimidine Dimer); Endodeoxyribonucleases/chemistry; Escherichia coli Proteins; Helix-Turn-Helix Motifs; Humans; Insect Proteins/chemistry; Molecular Sequence Data; N-Glycosyl Hydrolases/chemistry; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Sequence Homology, Amino Acid |
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