7JTU

Cytidine deaminase T6S toxin from Pseudomonas syringae

Summary for 7JTU

• Entry DOI: 10.2210/pdb7jtu/pdb
• Descriptor: SsdA, SsdAI (3 entities in total)
• Functional Keywords: toxin, immunity, type vi, t6ss, deaminase
• Biological source: Pseudomonas syringae; More
• Total number of polymer chains: 2
• Total formula weight: 40617.57

Authors

Bosch, D.E.,Hsu, F.,de Moraes, M.H.,Mougous, J.D. (deposition date: 2020-08-18, release date: 2021-03-31, Last modification date: 2024-11-20)

Primary citation

de Moraes, M.H.,Hsu, F.,Huang, D.,Bosch, D.E.,Zeng, J.,Radey, M.C.,Simon, N.,Ledvina, H.E.,Frick, J.P.,Wiggins, P.A.,Peterson, S.B.,Mougous, J.D.
An interbacterial DNA deaminase toxin directly mutagenizes surviving target populations.
Elife, 10:-, 2021

PubMed Abstract: When bacterial cells come in contact, antagonism mediated by the delivery of toxins frequently ensues. The potential for such encounters to have long-term beneficial consequences in recipient cells has not been investigated. Here, we examined the effects of intoxication by DddA, a cytosine deaminase delivered via the type VI secretion system (T6SS) of . Despite its killing potential, we observed that several bacterial species resist DddA and instead accumulate mutations. These mutations can lead to the acquisition of antibiotic resistance, indicating that even in the absence of killing, interbacterial antagonism can have profound consequences on target populations. Investigation of additional toxins from the deaminase superfamily revealed that mutagenic activity is a common feature of these proteins, including a representative we show targets single-stranded DNA and displays a markedly divergent structure. Our findings suggest that a surprising consequence of antagonistic interactions between bacteria could be the promotion of adaptation via the action of directly mutagenic toxins.

PubMed: 33448264
DOI: 10.7554/eLife.62967

Experimental method

X-RAY DIFFRACTION (3 Å)