6D0I

ParT: Prs ADP-ribosylating toxin bound to cognate antitoxin ParS. L48M ParT, SeMet-substituted complex.

Summary for 6D0I

• Entry DOI: 10.2210/pdb6d0i/pdb
• Descriptor: ParT: COG5654 (RES domain) toxin, ParS: COG5642 (DUF2384) antitoxin fragment, GLYCEROL, ... (4 entities in total)
• Functional Keywords: adp-ribosyltransferase, toxin-antitoxin complex, parst, toxin
• Biological source: Sphingobium sp. YBL2; More
• Total number of polymer chains: 4
• Total formula weight: 50311.69

Authors

Piscotta, F.J.,Jeffrey, P.D.,Link, A.J. (deposition date: 2018-04-10, release date: 2019-01-09, Last modification date: 2024-10-23)

Primary citation

Piscotta, F.J.,Jeffrey, P.D.,Link, A.J.
ParST is a widespread toxin-antitoxin module that targets nucleotide metabolism.
Proc. Natl. Acad. Sci. U.S.A., 116:826-834, 2019

PubMed Abstract: Toxin-antitoxin (TA) systems interfere with essential cellular processes and are implicated in bacterial lifestyle adaptations such as persistence and the biofilm formation. Here, we present structural, biochemical, and functional data on an uncharacterized TA system, the COG5654-COG5642 pair. Bioinformatic analysis showed that this TA pair is found in 2,942 of the 16,286 distinct bacterial species in the RefSeq database. We solved a structure of the toxin bound to a fragment of the antitoxin to 1.50 Å. This structure suggested that the toxin is a mono-ADP-ribosyltransferase (mART). The toxin specifically modifies phosphoribosyl pyrophosphate synthetase (Prs), an essential enzyme in nucleotide biosynthesis conserved in all organisms. We propose renaming the toxin ParT for Prs ADP-ribosylating toxin and ParS for the cognate antitoxin. ParT is a unique example of an intracellular protein mART in bacteria and is the smallest known mART. This work demonstrates that TA systems can induce bacteriostasis through interference with nucleotide biosynthesis.

PubMed: 30598453
DOI: 10.1073/pnas.1814633116

Experimental method

X-RAY DIFFRACTION (1.55 Å)