The structure of isometric capsids of bacteriophage T4.
The structure of isometric capsids of bacteriophage T4.
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DOI：
10.1006/viro.2000.0735
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发表时间：
2001-01
期刊：
影响因子：
3.7
通讯作者：
N. Olson;M. Gingery;F. Eiserling;T. Baker
中科院分区：
文献类型：
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作者：
N. Olson;M. Gingery;F. Eiserling;T. Baker
通过冷冻电子显微镜和图像重建技术确定了DNA填充的噬菌体T4等轴衣壳的三维结构。蛋白质亚基在衣壳表面上的堆积几何形状被确认为三角形类T = 13。重建清楚地显示了五聚体，归因于衣壳蛋白gp 24 *，被主要衣壳蛋白gp 23 * 的六聚体包围。辅助蛋白，Hoc和Soc的位置，也清楚地描绘在表面晶格。Hoc蛋白是最突出的表面特征，表现为具有圆形基部的延伸分子，从该基部突出细颈和球状头部。一个Hoc分子与每个六聚体缔合。通过12个Soc分子的缔合在gp 23 * 六聚体的外围形成几乎连续的“脊”;然而，Soc沿着六聚体和五聚体之间的边界不存在。双链DNA基因组形成一系列高度浓缩的同心层，间隔约2.36 nm，遵循蛋白质衣壳内壁的一般轮廓。
The three-dimensional structure of DNA-filled, bacteriophage T4 isometric capsids has been determined by means of cryoelectron microscopy and image reconstruction techniques. The packing geometry of protein subunits on the capsid surface was confirmed to be that of the triangulation class T = 13. The reconstruction clearly shows pentamers, attributed to capsid protein gp24*, surrounded by hexamers of the major capsid protein, gp23*. Positions of the accessory proteins, Hoc and Soc, are also clearly delineated in the surface lattice. The Hoc protein is the most prominent surface feature and appears as an extended molecule with a rounded base from which a thin neck and a globular head protrude. One Hoc molecule associates with each hexamer. Nearly continuous "ridges" are formed at the periphery of the gp23* hexamers by an association of 12 Soc molecules; however, Soc is absent along the boundaries between the hexamers and the pentamers. The duplex DNA genome forms a highly condensed series of concentric layers, spaced about 2.36 nm apart, that follow the general contour of the inner wall of the protein capsid.