6DRH

ADP-ribosyltransferase toxin/immunity pair

6DRH の概要

• エントリーDOI: 10.2210/pdb6drh/pdb
• 分子名称: ADP-ribosyl-(Dinitrogen reductase) hydrolase, PAAR repeat-containing protein, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: toxin, immunity, type vi secretion, adp-ribosyltransferase
• 由来する生物種: Serratia proteamaculans (strain 568); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 247668.74

構造登録者

Bosch, D.E.,Ting, S.,Allaire, M.,Mougous, J.D. (登録日: 2018-06-11, 公開日: 2018-10-31, 最終更新日: 2023-10-11)

主引用文献

Ting, S.Y.,Bosch, D.E.,Mangiameli, S.M.,Radey, M.C.,Huang, S.,Park, Y.J.,Kelly, K.A.,Filip, S.K.,Goo, Y.A.,Eng, J.K.,Allaire, M.,Veesler, D.,Wiggins, P.A.,Peterson, S.B.,Mougous, J.D.
Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins.
Cell, 175:1380-, 2018

PubMed Abstract: ADP-ribosylation of proteins can profoundly impact their function and serves as an effective mechanism by which bacterial toxins impair eukaryotic cell processes. Here, we report the discovery that bacteria also employ ADP-ribosylating toxins against each other during interspecies competition. We demonstrate that one such toxin from Serratia proteamaculans interrupts the division of competing cells by modifying the essential bacterial tubulin-like protein, FtsZ, adjacent to its protomer interface, blocking its capacity to polymerize. The structure of the toxin in complex with its immunity determinant revealed two distinct modes of inhibition: active site occlusion and enzymatic removal of ADP-ribose modifications. We show that each is sufficient to support toxin immunity; however, the latter additionally provides unprecedented broad protection against non-cognate ADP-ribosylating effectors. Our findings reveal how an interbacterial arms race has produced a unique solution for safeguarding the integrity of bacterial cell division machinery against inactivating post-translational modifications.

PubMed: 30343895
DOI: 10.1016/j.cell.2018.09.037

実験手法

X-RAY DIFFRACTION (2.299 Å)