Crystallization of parasporin-2, a Bacillus thuringiensis crystal protein with selective cytocidal activity against human cells
Crystallization of parasporin-2, a Bacillus thuringiensis crystal protein with selective cytocidal activity against human cells
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DOI：
10.1107/s0907444904026307
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发表时间：
2004-12-01
影响因子：
2.2
通讯作者：
Harata, K
中科院分区：
文献类型：
--
作者：
Akiba, T;Abe, Y;Harata, K
苏云金芽孢杆菌是一种有价值的蛋白质毒素来源，对某些昆虫和蠕虫特别有效，但对哺乳动物无害。相反，从B.苏云金菌株A1547，命名为副孢蛋白-2，不具有杀虫性，但对具有明显不同靶特异性的人细胞具有强的杀细胞活性。37 kDa的无活性蛋白质被蛋白水解活化为30 kDa的活性形式。重组蛋白毒素的活性形式在乙二醇和聚乙二醇8000存在下在中性pH下结晶，晶体属于六方空间群P6（1）或P6（5），晶胞参数a = B = 134.37，c = 121.24埃。使用同步辐射源收集天然晶体的衍射数据，分辨率为2.75埃。
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.