CRYSTALLINE ACTIN SHEETS - THEIR STRUCTURE AND POLYMORPHISM
CRYSTALLINE ACTIN SHEETS - THEIR STRUCTURE AND POLYMORPHISM
复制标题
DOI：
10.1083/jcb.91.2.340
复制
发表时间：
1981-01-01
影响因子：
7.8
通讯作者：
SMITH, PR
中科院分区：
文献类型：
--
作者：
AEBI, U;FOWLER, WE;SMITH, PR
三价镧系元素钆诱导的阿米巴肌动蛋白结晶片以3种不同的多晶型存在，表现出不同的条纹图案和表面形貌。这些不同的形式被称为矩形和正方形片，和圆柱体。这三种形式中的每一种都是由以不同方式关联的公共基本格构造而成的。电子显微照片的图像处理被用来获得一个模型的肌动蛋白分子在投影到1.5 nm的分辨率。在这些图像中观察到的总尺寸为5.6 × 104。3.3. times. 4.5 nm，并且分子本身明显地呈现出两叶，两个叶被裂缝分开。肌动蛋白单体在片排列与P2对称性和包装不同的分子在肌动蛋白丝。因为. apprx.由于肌动蛋白分子的35%的表面积暴露在这些薄片的表面上，因此这些薄片应该可用于研究肌动蛋白结合蛋白与肌动蛋白分子的化学计量结合。
Crystalline sheets of Acanthamoeba actin induced by the trivalent lanthanide gadolinium exist in 3 different polymorphic forms, which show different striation patterns and surface topographies. These different forms are called rectangular and square sheets, and cylinders. Each of the 3 forms is constructed from common basic lattices associated in different ways. Image processing of electron micrographs was used to obtain a model for the actin molecule in projection to a resolution of 1.5 nm. The overall dimensions observed in these images are 5.6 .times. 3.3 .times. 4.5 nm, and the molecule itself appears distinctly bilobed with the 2 lobes separated by a cleft. Actin monomers in the sheets are arranged with P2 symmetry and are packed differently from the molecules in actin filaments. Because .apprx. 35% of the surface area of the actin molecule is exposed on the surface of these sheets, the sheets should be useful to study the stoichiometric binding of actin-binding proteins to the actin molecule.