Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1.
Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1.
复制标题
1型单纯疱疹病毒UL6门户蛋白的结构和多态性。
DOI：
10.1128/jvi.78.22.12668-12671.2004
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发表时间：
2004
影响因子：
5.4
通讯作者：
Steven,AlasdairC
中科院分区：
文献类型：
--
作者：
Trus,BenesL;Cheng,Naiqian;Newcomb,WilliamW;Homa,FredL;Brown,JayC;Steven,AlasdairC
通过电子显微镜和图像分析，我们发现杆状病毒表达的UL 6是多态性的，由11-，12-，13-和14-倍对称的环组成。12聚体可能是低聚物纳入原衣壳：在16埃的分辨率，它有一个轴向通道，周边凸缘，并适合紧贴到一个空置的顶点网站。它的结构类似于噬菌体门户/连接蛋白。
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 Å, it has an axial channel, peripheral flanges, and fits snugly into a vacant vertex site. Its architecture resembles those of bacteriophage portal/connector proteins.