PMID:10679272

Citation	Plochocka, D, Kierzek, A, Obtulowicz, T, Tudek, B and Zielenkiewicz, P (2000) 3-Methyladenine-DNA glycosylase I from Escherichia coli-computer modeling and supporting experimental evidence. Biochem. Biophys. Res. Commun. 268:724-7
Abstract	TagA (3-methyladenine-DNA glycosylase I) excises 3-methyadenine and 3-methylguanine from alkylated DNA. The structure of this enzyme has not yet been determined experimentally. We propose a three-dimensional model of the TagA protein based on the threading algorithm. The model shows that TagA is a mostly alpha-helical protein, in agreement with circular dichroism measurements. None of the eight cysteines present in the TagA sequence forms a disulfide bridge in the model structure, which has also been experimentally verified with the use of Ellman method.
Links	PubMed Online version:10.1006/bbrc.2000.2116
Keywords	Algorithms; Amino Acid Sequence; Circular Dichroism; Computer Simulation; Cysteine/chemistry; DNA Glycosylases; Disulfides/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Models, Molecular; Molecular Sequence Data; N-Glycosyl Hydrolases/chemistry; N-Glycosyl Hydrolases/genetics; Protein Conformation; Protein Structure, Secondary; Sequence Homology, Amino Acid
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