Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli

Yuriko Yamagata, Masato Kato, Kyoko Odawara, Yoshiteru Tokuno, Yoko Nakashima, Nobuko Matsushima, Kohei Yasumura, Ken Ichi Tomita, Kenji Ihara, Yoshimitsu Fujii, Yusaku Nakabeppu, Mutsuo Sekiguchi, Satoshi Fujii

Research output: Contribution to journalArticle

122 Scopus citations

Abstract

The three-dimensional structure of Escherichia coli 3-methyladenine DNA glycosylase II, which removes numerous alkylated bases from DNA, was solved at 2.3 Å resolution. The enzyme consists of three domains: one α + β fold domain with a similarity to one-half of the eukaryotic TATA box-binding protein, and two all α-helical domains similar to those of Escherichia coli endonuclease III with combined N-glycosylase/abasic lyase activity. Mutagenesis and model-building studies suggest that the active site is located in a cleft between the two helical domains and that the enzyme flips the target base out of the DNA duplex into the active-site cleft. The structure of the active site implies broad substrate specificity and simple N-glycosylase activity.

Original languageEnglish (US)
Pages (from-to)311-319
Number of pages9
JournalCell
Volume86
Issue number2
DOIs
StatePublished - Jul 26 1996

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Yamagata, Y., Kato, M., Odawara, K., Tokuno, Y., Nakashima, Y., Matsushima, N., Yasumura, K., Tomita, K. I., Ihara, K., Fujii, Y., Nakabeppu, Y., Sekiguchi, M., & Fujii, S. (1996). Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli. Cell, 86(2), 311-319. https://doi.org/10.1016/S0092-8674(00)80102-6