7ZHM

Salmonella enterica Rhs1 C-terminal toxin TreTu complex with TriTu immunity protein

Summary for 7ZHM

• Entry DOI: 10.2210/pdb7zhm/pdb
• Descriptor: Rhs1 protein, Immunity protein TriTu, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total)
• Functional Keywords: bacterial toxin, toxin-immunity, secreted toxin, t6ss, rhs, toxin
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium; More
• Total number of polymer chains: 4
• Total formula weight: 47069.08

Authors

Jurenas, D.,Rey, M.,Chamot-Rooke, J.,Terradot, L.,Cascales, E. (deposition date: 2022-04-06, release date: 2022-11-23, Last modification date: 2024-05-01)

Primary citation

Jurenas, D.,Rey, M.,Byrne, D.,Chamot-Rooke, J.,Terradot, L.,Cascales, E.
Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop.
Nucleic Acids Res., 50:13114-13127, 2022

PubMed Abstract: Rearrangement hot spot (Rhs) proteins are members of the broad family of polymorphic toxins. Polymorphic toxins are modular proteins composed of an N-terminal region that specifies their mode of secretion into the medium or into the target cell, a central delivery module, and a C-terminal domain that has toxic activity. Here, we structurally and functionally characterize the C-terminal toxic domain of the antibacterial Rhsmain protein, TreTu, which is delivered by the type VI secretion system of Salmonella enterica Typhimurium. We show that this domain adopts an ADP-ribosyltransferase fold and inhibits protein synthesis by transferring an ADP-ribose group from NAD+ to the elongation factor Tu (EF-Tu). This modification is specifically placed on the side chain of the conserved D21 residue located on the P-loop of the EF-Tu G-domain. Finally, we demonstrate that the TriTu immunity protein neutralizes TreTu activity by acting like a lid that closes the catalytic site and traps the NAD+.

PubMed: 36484105
DOI: 10.1093/nar/gkac1162

Experimental method

X-RAY DIFFRACTION (2.7 Å)