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一个β-螺旋环抗蛋白的表面基和水模仿冰结构

Y C Liou¹, A Tocilj, P L Davies

¹Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.

|August 5, 2000

概括

来自甲虫的昆虫抗蛋白 (AFP) 在防止冰晶生长方面非常有效. 坦尼布里奥摩利托 AFP 结构揭示了一个异常规律的β螺旋,具有独特的结冰表面.

科学领域:

生物化学生物化学
结构生物学结构生物学
低温生物学低温生物学

背景情况:

与鱼类的抗蛋白相比,昆虫的抗蛋白 (AFP) 显示出更高的点压力.
甲虫Tenebrio molitor拥有具有高冰增长抑制功效的AFP.

研究的目的:

为了确定Tenebrio molitor AFP的高分辨率晶体结构.
阐明这种昆虫AFP强大的抗活性的结构基础.

主要方法:

在1.4-A分辨率的X射线晶体学.
蛋白质结构的分析,包括二次结构,结合和侧链形状.

主要成果:

坦尼布里奥摩利图尔 (Tenebrio molitor AFP) 采用了一个异常规律的β螺旋结构.
蛋白质通过二硫化物和键稳定,缺乏显著的疏水核.
一个保存的三氨酸-氨酸-三氨酸图案形成一个平坦的β片,被确定为假定的结冰表面.
氨酸侧链和结合的水分子模仿冰格结构.

结论:

斑菌的高度规律的β螺旋结构是其强大的抗活性的关键.
氨酸残留物和相关的水分子的特定排列提供了与冰网的近乎完美的匹配,从而能够有效地抑制冰的生长.

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