Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila.

ABSTRACT: Toxin-antitoxin (TA) systems are ubiquitous genetic modules in bacteria and archaea. Here, we perform structural and biochemical characterization of the Legionella pneumophila effector Lpg2370, demonstrating that it is a Ser/Thr kinase. Together with two upstream genes, lpg2370 constitutes the tripartite HipBST TA. Notably, the toxin Lpg2370 (HipT_Lp) and the antitoxin Lpg2369 (HipS_Lp) correspond to the C-terminus and N-terminus of HipA from HipBA TA, respectively. By determining crystal structures of autophosphorylated HipT_Lp, its complex with AMP-PNP, and the structure of HipT_Lp-HipS_Lp complex, we identify residues in HipT_Lp critical for ATP binding and those contributing to its interactions with HipS_Lp. Structur

SUBMITTER: Zhen X 

PROVIDER: S-EPMC9325769 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature