6D0H
ParT: Prs ADP-ribosylating toxin bound to cognate antitoxin ParS
6D0H の概要
エントリーDOI | 10.2210/pdb6d0h/pdb |
分子名称 | ParT: COG5654 (RES domain) toxin, ParS: COG5642 (DUF2384) antitoxin, GLYCEROL, ... (4 entities in total) |
機能のキーワード | adp-ribosyltransferase, toxin-antitoxin complex, parst, toxin |
由来する生物種 | Sphingobium sp. YBL2 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 49992.55 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 30598453DOI: 10.1073/pnas.1814633116 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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