IMAGE-RECONSTRUCTION REVEALS THE COMPLEX MOLECULAR-ORGANIZATION OF ADENOVIRUS
IMAGE-RECONSTRUCTION REVEALS THE COMPLEX MOLECULAR-ORGANIZATION OF ADENOVIRUS
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DOI：
10.1016/0092-8674(91)90578-m
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发表时间：
1991-10-04
期刊：
影响因子：
64.5
通讯作者：
FULLER, SD
中科院分区：
文献类型：
--
作者：
STEWART, PL;BURNETT, RM;FULLER, SD
腺病毒的三维结构已被确定的图像重建从冷冻电子显微镜。与主要衣壳蛋白hexon的高分辨率x射线晶体结构进行比较，可以对密度图进行异常详细的解释，并证实了重建的有效性。在衣壳内的六方体填料显示出比以前提出的更广泛的面之间的分子间界面。重建提供了顶点蛋白的第一个三维可视化，包括五边形碱基及其相关的突出纤维。揭示了稳定和调节衣壳体相互作用的三种次要衣壳蛋白。其中一个组件稳定每个面中心的9个六边形和相邻面的另外两个桥六边形。这些蛋白质的战略位置突出了胶凝蛋白在稳定复杂组装中的重要性。
The three-dimensional structure of adenovirus has been determined by image reconstruction from cryoelectron micrographs. Comparison with the high resolution X-ray crystal structure of hexon, the major capsid protein, enabled an unusually detailed interpretation of the density map and confirmed the validity of the reconstruction. The hexon packing in the capsid shows more extensive intermolecular interfaces between facets than previously proposed. The reconstruction provides the first three-dimensional visualization of the vertex proteins, including the penton base and its associated protruding fiber. Three minor capsid proteins that stabilize and modulate capsomer interactions are revealed. One of these components stabilizes the group-of-nine hexons in the center of each facet and the other two bridge hexons in adjacent facets. The strategic positions of these proteins highlight the importance of cementing proteins in stabilizing a complex assembly.