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

研究成果: Contribution to journalArticle査読

128 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)311-319
ページ数9
ジャーナルCell
86
2
DOI
出版ステータス出版済み - 7 26 1996

All Science Journal Classification (ASJC) codes

  • 生化学、遺伝学、分子生物学(全般)

フィンガープリント

「Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル