VI型分泌系统
分泌物
铜绿假单胞菌
穿刺
Spike(软件开发)
生物
效应器
三型分泌系统
细菌
生物物理学
细胞生物学
微生物学
化学
生物化学
遗传学
计算机科学
毒力
基因
软件工程
电信
作者
Mercedes Spínola-Amilibia,Irene Davó-Siguero,Federico M. Ruiz,Elena Santillana,F.J. Medrano,Antonio Romero
出处
期刊:Acta Crystallographica Section D: Structural Biology
[Wiley]
日期:2016-01-01
卷期号:72 (1): 22-33
被引量:33
标识
DOI:10.1107/s2059798315021142
摘要
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-(gp5)3 puncturing complex. Here, the crystal structure of full-length VgrG1 from Pseudomonas aeruginosa is reported at a resolution of 2.0 Å, which through a trimeric arrangement generates a needle-like shape composed of two main parts, the head and the spike, connected 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 β-roll spike with implications in the cell-membrane puncturing process and as a carrier of cognate toxins.
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