A putative membrane-associated YdjB-like protein from Salmonella enterica exhibits a non-canonical ACT-like fold.

ABSTRACT: The Aspartokinase-Chorismate mutase-TyrA (ACT) domain is a conserved regulatory module found in a wide range of proteins involved in diverse biological processes, including amino acid metabolism, signal transduction, and cytoskeletal organization. Despite extensive studies, the structural and functional diversity of ACT domains continues to expand. Here, we present the high-resolution crystal structure of an 18 kDa YdjB-like protein from Salmonella enterica (seYdjB-like protein), a conserved but previously uncharacterized ACT domain-containing protein. Structural analysis reveals a novel ACT-like fold distinct from canonical ACT domains, despite superficial resemblance to aspartokinase. Interestingly, seYdjB-like protein forms a stable dimer in solution and is predicted to be associated wi

SUBMITTER: Kim JH 

PROVIDER: S-EPMC12697964 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature