Crystallization and preliminary X-ray diffraction analysis of spermidine synthase from Helicobacter pylori

被引：5

作者：

Lu, PK

Chien, SY

Tsai, JY

Fong, CT

Lee, MJ

Huang, H

Sun, YJ ^{[1
]}

机构：

[1] Natl Tsing Hua Univ, Inst Bioinformat & Struct Biol, Hsinchu 300, Taiwan

[2] Natl Tsing Hua Univ, Inst Biotechnol, Hsinchu 300, Taiwan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷

关键词：

D O I：

10.1107/S0907444904021985

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Polyamines, such as putrescine, spermidine and spermine, are essential for the regulation of cell proliferation and differentiation in most organisms. Spermidine synthase catalyzes the transfer of the aminopropyl group from decarboxylated S-adenosylmethionine to putrescine in the biosynthesis of spermidine. In this study, spermidine synthase of Helicobacter pylori has been overexpressed in Escherichia coli and purified. Two kinds of spermidine synthase crystals were obtained. One belongs to the monoclinic P2(1) space group, with unit-cell parameters a=62.78, b=58.24, c=74.28 Angstrom, beta=90.9, and the other belongs to the orthorhombic C222(1) space group, with unit-cell parameters a=100.43, b=128.55, c=143.60 Angstrom.

引用

页码：2067 / 2069

页数：3

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