4ZV0

Structure of Tse6 in complex with Tsi6

Summary for 4ZV0

• Entry DOI: 10.2210/pdb4zv0/pdb
• Related: 4ZUY 4ZV4
• Descriptor: antibacterial effector secreted protein (type VI secretion system), Tse6-binding/Tse6 immunity protein, IODIDE ION, ... (4 entities in total)
• Functional Keywords: t6ss effector-immunity pair, protein binding
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228); More
• Total number of polymer chains: 2
• Total formula weight: 30291.92

Authors

Whitney, J.C.,Sawai, S.,Ralston, C.,Mougous, J.D. (deposition date: 2015-05-18, release date: 2015-11-11, Last modification date: 2024-11-06)

Primary citation

Whitney, J.C.,Quentin, D.,Sawai, S.,LeRoux, M.,Harding, B.N.,Ledvina, H.E.,Tran, B.Q.,Robinson, H.,Goo, Y.A.,Goodlett, D.R.,Raunser, S.,Mougous, J.D.
An Interbacterial NAD(P)(+) Glycohydrolase Toxin Requires Elongation Factor Tu for Delivery to Target Cells.
Cell, 163:607-619, 2015

PubMed 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.

PubMed: 26456113
DOI: 10.1016/j.cell.2015.09.027

Experimental method

X-RAY DIFFRACTION (1.401 Å)