3-methyladenine-DNA glycosylase I from Escherichia coli - Computer modeling and supporting experimental evidence

Citation
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
ISSN journal
0006291X → ACNP
Volume
268
Issue
3
Year of publication
2000
Pages
724 - 727
Database
ISI
SICI code
0006-291X(20000224)268:3<724:3GIFEC>2.0.ZU;2-Z
Abstract
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.