EMD-3113

Single-particle
21.5 Å
EMD-3113 Deposition: 06/08/2015
Map released: 21/10/2015
Last modified: 25/11/2015
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-3113

Negative stain EM structure of the Tse6-Tsi6-VgrG1-EagT6-EF-Tu complex

EMD-3113

Single-particle
21.5 Å
EMD-3113 Deposition: 06/08/2015
Map released: 21/10/2015
Last modified: 25/11/2015
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Pseudomonas aeruginosa PAO1, Escherichia coli
Sample: Tse6-Tsi6-VgrG1-EagT6-EF-Tu complex

Deposition Authors: Whitney J, Quentin D , Sawai S, LeRoux M , Harding B, Ledvina H , Tran B, Robinson H, Goo YA, Goodlett D, Raunser S , Mougous J
An Interbacterial NAD(P) Glycohydrolase Toxin Requires Elongation Factor Tu for Delivery to Target Cells.
Abstract:
Type VI secretion (T6S) influences the composition of microbial communities by catalyzing the delivery of toxins between adjacent bacterial cells. Here, we demonstrate that a T6S integral membrane toxin from Pseudomonas aeruginosa, Tse6, acts on target cells by degrading the universally essential dinucleotides NAD(+) and NADP(+). Structural analyses of Tse6 show that it resembles mono-ADP-ribosyltransferase proteins, such as diphtheria toxin, with the exception of a unique loop that both excludes proteinaceous ADP-ribose acceptors and contributes to hydrolysis. We find that entry of Tse6 into target cells requires its binding to an essential housekeeping protein, translation elongation factor Tu (EF-Tu). These proteins participate in a larger assembly that additionally directs toxin export and provides chaperone activity. Visualization of this complex by electron microscopy defines the architecture of a toxin-loaded T6S apparatus and provides mechanistic insight into intercellular membrane protein delivery between bacteria.