4ZUY

Structure of Tsi6 from Pseudomonas aeruginosa

Summary for 4ZUY

• Entry DOI: 10.2210/pdb4zuy/pdb
• Related: 4ZV0 4ZV4
• Descriptor: Tsi6, CHLORIDE ION (3 entities in total)
• Functional Keywords: 4-helix bundle, bacterial type vi secretion immunity protein, tse6 immunity protein, protein binding
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
• Total number of polymer chains: 2
• Total formula weight: 23894.42

Authors

Whitney, J.C.,Sawai, S.,Robinson, H.,Mougous, J.D. (deposition date: 2015-05-18, release date: 2015-11-11, Last modification date: 2024-10-23)

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 (1.952 Å)