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- Title
The structure of VgrG1 from Pseudomonas aeruginosa Pseudomonas aeruginosa, the needle tip of the bacterial type VI secretion system.
- Authors
Spínola-Amilibia, Mercedes; Davó-Siguero, Irene; Ruiz, Federico M.; Santillana, Elena; Medrano, Francisco Javier; Romero, Antonio
- Abstract
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 from Pseudomonas aeruginosa 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 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.
- Subjects
BACTERIAL protein structure; PSEUDOMONAS aeruginosa; X-ray crystallography
- Publication
Acta Crystallographica: Section D, Structural Biology, 2016, Vol 72, Issue 1, p22
- ISSN
0907-4449
- Publication type
Article
- DOI
10.1107/S2059798315021142