4ZV4
Structure of Tse6 in complex with EF-Tu
Summary for 4ZV4
| Entry DOI | 10.2210/pdb4zv4/pdb |
| Related | 4ZUY 4ZV0 |
| Descriptor | Elongation factor Tu, Tse6, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | t6ss effector, translation elongation factor, translation |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) More |
| Total number of polymer chains | 4 |
| Total formula weight | 130172.71 |
| Authors | Whitney, J.C.,Sawai, S.,Robinson, H.,Mougous, J.D. (deposition date: 2015-05-18, release date: 2015-11-11, Last modification date: 2023-09-27) |
| 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 Cited by 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: 26456113DOI: 10.1016/j.cell.2015.09.027 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.504 Å) |
Structure validation
Download full validation report
