D. Plochocka et al., 3-methyladenine-DNA glycosylase I from Escherichia coli - Computer modeling and supporting experimental evidence, BIOC BIOP R, 268(3), 2000, pp. 724-727
Citations number
18
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
TagA (3-methyladenine-DNA glycosylase I) excises 3-methyadenine and 3-methy
lguanine 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 m
ostly alpha-helical protein, in agreement with circular dichroism measureme
nts. None of the eight cysteines present in the TagA sequence forms a disul
fide bridge in the model structure, which has also been experimentally veri
fied with the use of Ellman method. (C) 2000 Academic Press.