单纯疱疹病毒1型UL6门户蛋白的结构与多态性
Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1.
作者信息
Trus Benes L, Cheng Naiqian, Newcomb William W, Homa Fred L, Brown Jay C, Steven Alasdair C
机构信息
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Building 50, Room 1517, MSC 8025, 50 South Drive, Bethesda, MD 20892-8025, USA.
出版信息
J Virol. 2004 Nov;78(22):12668-71. doi: 10.1128/JVI.78.22.12668-12671.2004.
Abstract
By electron microscopy and image analysis, we find that baculovirus-expressed UL6 is polymorphic, consisting of rings of 11-, 12-, 13-, and 14-fold symmetry. The 12-mer is likely to be the oligomer incorporated into procapsids: at a resolution of 16 A, it has an axial channel, peripheral flanges, and fits snugly into a vacant vertex site. Its architecture resembles those of bacteriophage portal/connector proteins.
摘要
通过电子显微镜和图像分析，我们发现杆状病毒表达的UL6是多态性的，由具有11、12、13和14重对称性的环组成。12聚体可能是整合到原衣壳中的寡聚体：在16埃的分辨率下，它有一个轴向通道、外周凸缘，并且紧密地契合到一个空的顶点位点。其结构类似于噬菌体门户/连接蛋白的结构。
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