Crystallization of parasporin-2, a Bacillus thuringiensis crystal protein with selective cytocidal activity against human cells

被引：5

作者：

Akiba, T

Abe, Y

Kitada, S

Kusaka, Y

Ito, A

Ichimatsu, T

Katayama, H

Akao, T

Higuchi, K

Mizuki, E

Ohba, M

Kanai, R

Harata, K ^{[1
]}

机构：

[1] AIST, Biol Informat Res Ctr, Tsukuba, Ibaraki 3058566, Japan

[2] Kyushu Univ, Fac Sci, Dept Chem, Fukuoka 8128581, Japan

[3] Fukuoka Ind Technol Ctr, Biotechnol & Food Res Inst, Fukuoka 8390861, Japan

[4] Kyushu Univ, Fac Agr, Dept Appl Genet & Pest Management, Fukuoka 8128581, Japan

来源：

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

关键词：

D O I：

10.1107/S0907444904026307

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Bacillus thuringiensis is a valuable source of protein toxins that are specifically effective against certain insects and worms but harmless to mammals. In contrast, a protein toxin obtained from B. thuringiensis strain A1547, designated parasporin-2, is not insecticidal but has a strong cytocidal activity against human cells with markedly divergent target specificity. The 37 kDa inactive protein is proteolytically activated to a 30 kDa active form. The active form of the recombinant protein toxin was crystallized in the presence of ethylene glycol and polyethylene glycol 8000 at neutral pH. The crystals belong to the hexagonal space group P6(1) or P6(5), with unit-cell parameters a = b = 134.37, c = 121.24 Angstrom. Diffraction data from a native crystal were collected to 2.75 Angstrom resolution using a synchrotron-radiation source.

引用

页码：2355 / 2357

页数：3

共 22 条

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