The structure of VgrG1 from Pseudomonas aeruginosa, the needle tip of the bacterial type VI secretion system
The structure of VgrG1 from Pseudomonas aeruginosa, the needle tip of the bacterial type VI secretion system
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DOI：
10.1107/s2059798315021142
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发表时间：
2016-01-01
影响因子：
2.2
通讯作者：
Romero, Antonio
中科院分区：
文献类型：
--
作者：
Spinola-Amilibia, Mercedes;Davo-Siguero, Irene;Romero, Antonio
VI型分泌系统（T6 SS）是病原菌感染宿主细胞和在竞争环境中生存的常用机制。该系统在核心基板上组装并像噬菌体穿刺装置一样伸长;它被认为穿透靶膜并将效应物递送到宿主或竞争细菌中。缬氨酸-甘氨酸重复蛋白G1（VgrG 1）在溶血素共调节蛋白1（Hcp 1）形成的延伸管尖端形成刺突;它在结构上类似于T4噬菌体（gp 27）（3 3）-（gp 5）（3 3）穿刺复合物。在这里，来自铜绿假单胞菌的全长VgrG 1的晶体结构以2.0埃的分辨率被报道，它通过三聚体排列产生由两个主要部分组成的针状形状，头部和尖峰，通过一个小的颈部区域连接。该结构揭示了几个显着的结构特征，指向VgrG 1的两个主要部分的可能作用：作为支架货物结构域的头部和卷穗与细胞膜穿刺过程中的影响，并作为同源毒素的载体。
The type VI secretion system (T6SS) is a mechanism that is commonly used by pathogenic bacteria to infect host cells and for survival in competitive environments. This system assembles on a core baseplate and elongates like a phage puncturing device; it is thought to penetrate the target membrane and deliver effectors into the host or competing bacteria. Valine-glycine repeat protein G1 (VgrG1) forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein 1 (Hcp1); it is structurally similar to the T4 phage (gp27)(3 3)-(gp5)(3 3) puncturing complex. Here, the crystal structure of full-length VgrG1 fromPseudomonas aeruginosa Pseudomonas aeruginosa is reported at a resolution of 2.0 angstrom, which through a trimeric arrangement generates a needle-like shape composed of two main parts, the head and the spike, connectedvia via a small neck region. The structure reveals several remarkable structural features pointing to the possible roles of the two main segments of VgrG1: the head as a scaffold cargo domain and the -roll spike with implications in the cell-membrane puncturing process and as a carrier of cognate toxins.