A three-dimensional cryo-electron microscopy structure of the bacteriophage φKZ head
A three-dimensional cryo-electron microscopy structure of the bacteriophage φKZ head
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DOI：
10.1016/j.jmb.2005.07.018
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发表时间：
2005-09-09
影响因子：
5.6
通讯作者：
Mesyanzhinov, VV
中科院分区：
文献类型：
--
作者：
Fokine, A;Kostyuchenko, VA;Mesyanzhinov, VV
用冷冻电子显微镜和图像重建技术测定了铜绿假单胞菌噬菌体Phi KZ头的三维结构，得到了18(A)的圆分辨率。头部具有二十面体对称性，直径为1455(A)，沿5个轴向为圆形，并有一个独特的门状顶点，其上连接着一个约1800(A)的圆形长收缩尾巴。65 kDa的主要衣壳蛋白gp120被组织成一个六角体的表面晶格，T=27三角。六聚体的形状和大小类似于噬菌体T4、Phi 29、P22和HK97的六聚体构建块。衣壳的五聚体顶端被几种特殊的顶端蛋白组成的复合体占据。双链基因组DNA被包装成高度浓缩的一系列层，由24(A)上的圆圈隔开，沿着衣壳内壁的轮廓。(C)2005爱思唯尔有限公司。保留所有权利。
The three-dimensional structure of the Pseudomonas aeruginosa bacteriophage Phi KZ head has been determined by cryo-electron microscopy and image reconstruction to 18 (A) over circle resolution. The head has icosahedral symmetry measuring 1455 (a) over circle in diameter along 5-fold axes and a unique portal vertex to which is attached an approximately 1800 (A) over circle -long contractile tail. The 65 kDa major capsid protein, gp120, is organized into a surface lattice of hexamers, with T=27 triangulation. The shape and size of the hexamers is similar to the hexameric building blocks of the bacteriophages T4, Phi 29, P22, and HK97. Pentameric vertices of the capsid are occupied by complexes composed of several special vertex proteins. The double-stranded genomic DNA is packaged into a highly condensed series of layers, separated by 24 (A) over circle, that follow the contour of the inner wall of the capsid. (c) 2005 Elsevier Ltd. All rights reserved.