Tetrameric structure of Bacillus subtilis DegQ and its predicted interaction with the DegS-DegU two-component system.

ABSTRACT: Bacillus subtilis DegQ is a 46-amino-acid regulatory protein involved in the DegS-DegU two-component system. DegQ promotes the phosphorylation of DegU by DegS, switching the function of DegU from competence to the induction of poly-γ-glutamate production. To elucidate its structural role, we determined the crystal structures of wild-type DegQ and its mutant DegQS25L. Each DegQ monomer folds into a single α-helix, and four monomers assemble into a tetramer characterized by a four-helix coiled-coil structure. Within the tetramer, two adjacent helices are oriented in the same direction, while the other two are oriented oppositely, forming a pseudo-twofold symmetric arrangement. The mutant form displays disrupted symmetry due to altered helix packing, which is caused by shifts in the coiled-co

SUBMITTER: Fujimoto Z 

PROVIDER: S-EPMC12485493 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature