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

被引：130

作者：

Yamagata, Y ^{[1
]}

Kato, M ^{[1
]}

Odawara, K ^{[1
]}

Tokuno, Y ^{[1
]}

Nakashima, Y ^{[1
]}

Matsushima, N ^{[1
]}

Yasumura, K ^{[1
]}

Tomita, K ^{[1
]}

Ihara, K ^{[1
]}

Fujii, Y ^{[1
]}

Nakabeppu, Y ^{[1
]}

Sekiguchi, M ^{[1
]}

Fujii, S ^{[1
]}

机构：

[1] KYUSHU UNIV,MED INST BIOREGULAT,HIGASHI KU,FUKUOKA 812,JAPAN

来源：

CELL | 1996年 / 86卷 / 02期

关键词：

D O I：

10.1016/S0092-8674(00)80102-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The three-dimensional structure of Escherichia coli 3-methyladenine DNA glycosylase II, which removes numerous alkylated bases from DNA, was solved at 2.3 Angstrom resolution. The enzyme consists of three domains: one alpha + beta fold domain with a similarity to one-half of the eukaryotic TATA box-binding protein, and two all alpha-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.

引用

页码：311 / 319

页数：9

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