作为一种特殊的F-肌动蛋白交联剂的绒毛蛋白的三维结构。
The 3D structure of villin as an unusual F-Actin crosslinker.
作者信息
Hampton Cheri M, Liu Jun, Taylor Dianne W, DeRosier David J, Taylor Kenneth A
机构信息
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, USA.
出版信息
Structure. 2008 Dec 10;16(12):1882-91. doi: 10.1016/j.str.2008.09.015.
Abstract
Villin is an F-actin nucleating, crosslinking, severing, and capping protein within the gelsolin superfamily. We have used electron tomography of 2D arrays of villin-crosslinked F-actin to generate 3D images revealing villin's crosslinking structure. In these polar arrays, neighboring filaments are spaced 125.9 +/- 7.1 A apart, offset axially by 17 A, with one villin crosslink per actin crossover. More than 6500 subvolumes containing a single villin crosslink and the neighboring actin filaments were aligned and classified to produce 3D subvolume averages. Placement of a complete villin homology model into the average density reveals that full-length villin binds to different sites on F-actin from those used by other actin-binding proteins and villin's close homolog gelsolin.
摘要
绒毛蛋白是凝溶胶蛋白超家族中的一种能使F-肌动蛋白成核、交联、切断和加帽的蛋白质。我们利用绒毛蛋白交联F-肌动蛋白二维阵列的电子断层扫描技术生成三维图像，揭示绒毛蛋白的交联结构。在这些极性阵列中，相邻细丝的间距为125.9±7.1埃，轴向偏移17埃，每个肌动蛋白交叉处有一个绒毛蛋白交联。对包含单个绒毛蛋白交联和相邻肌动蛋白细丝的6500多个子体积进行对齐和分类，以生成三维子体积平均值。将完整的绒毛蛋白同源模型放入平均密度中显示，全长绒毛蛋白与F-肌动蛋白上的结合位点不同于其他肌动蛋白结合蛋白以及绒毛蛋白的紧密同源物凝溶胶蛋白所使用的位点。
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