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首页> 外文期刊>Journal of Molecular Biology >The three-dimensional structure of the Limulus acrosomal process: a dynamic actin bundle.
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The three-dimensional structure of the Limulus acrosomal process: a dynamic actin bundle.

机译：mul顶体过程的三维结构：动态肌动蛋白束。

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摘要

Limulus sperm contains a dynamic macromolecular structure that rapidly extends a 50 &mgr;m process called the true discharge. The core of this structure is a bundle of ordered filaments composed of a complex of actin, scruin and calmodulin. We determined its structure by electron crystallographic reconstruction. The three-dimensional map reveals an actin-scruin helix that is azimuthally modulated by the influence of the interactions of a filament with its neighbors. There are a variety of density connections with neighboring filaments involving scruin. Scruin commonly contacts one neighbor, but we observe up to three interfilament connections involving both domains of the 28 scruin molecules in the unit cell. Our structure indicates that promiscuous scruin-scruin contacts are the major determinants of bundle stability in the true discharge. It also suggests that rearrangements would be permitted, which can facilitate the transition from the coiled to the true discharge form. Copyright 1999 Academic Press.
机译：精子包含一个动态的大分子结构，该结构迅速扩展了称为真正放电的50μm过程。这种结构的核心是一束有序的细丝，由肌动蛋白，细蛋白和钙调蛋白的复合物组成。我们通过电子晶体学重建确定其结构。三维图显示了肌动蛋白-螺旋结构螺旋，该螺旋结构受细丝与其邻居的相互作用的影响而被方位角调制。与邻近细丝的细丝存在多种密度连接。 Scruin通常会与一个邻居接触，但是我们观察到多达三个丝间连接，涉及单位细胞中28个scruin分子的两个结构域。我们的结构表明，混杂的sc- pro接触是真正放电中束稳定性的主要决定因素。还建议允许重排，这可以促进从盘绕到真正的放电形式的过渡。版权所有1999，学术出版社。

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