Crystal structure of family 4 uracil-DNA glycosylase from Sulfolobus tokodaii and a function of tyrosine 170 in DNA binding

被引：9

作者：

Kawai, Akito ^{[1
]}

Higuchi, Shigesada ^{[1
]}

Tsunoda, Masaru ^{[3
]}

Nakamura, Kazuo T. ^{[2
]}

Yamagata, Yuriko ^{[4
]}

Miyamoto, Shuichi ^{[1
]}

机构：

[1] Sojo Univ, Fac Pharmaceut Sci, Nishi Ku, Kumamoto 8600082, Japan

[2] Showa Univ, Sch Pharm, Shinagawa Ku, Tokyo 1428555, Japan

[3] Iwaki Meisei Univ, Fac Pharm, Iwaki, Fukushima 9708551, Japan

[4] Kumamoto Univ, Grad Sch Pharmaceut Sci, Chuo Ku, Kumamoto 8620973, Japan

来源：

FEBS LETTERS | 2015年 / 589卷 / 19期

关键词：

Uracil-DNA glycosylase; Crystal structure; Leucine-intercalation loop; Sulfolobus tokodaii; BASE EXCISION-REPAIR; SPECIFICITY;

D O I：

10.1016/j.febslet.2015.08.019

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：

Uracil-DNA glycosylases (UDGs) excise uracil from DNA by catalyzing the N-glycosidic bond hydrolysis. Here we report the first crystal structures of an archaeal UDG (stoUDG). Compared with other UDGs, stoUDG has a different structure of the leucine-intercalation loop, which is important for DNA binding. The stoUDG-DNA complex model indicated that Leu169, Tyr170, and Asn171 in the loop are involved in DNA intercalation. Mutational analysis showed that Tyr170 is critical for substrate DNA recognition. These results indicate that Tyr170 occupies the intercalation site formed after the structural change of the leucine-intercalation loop required for the catalysis. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2675 / 2682

页数：8

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