Mutant structure of metabolic switch protein in complex with monomeric c-di-GMP reveals a potential mechanism of protein-mediated ligand dimerization.

ABSTRACT: Bacterial second messengers c-di-GMP and (p)ppGpp have broad functional repertoires ranging from growth and cell cycle control to the regulation of biofilm formation and virulence. The recent identification of SmbA, an effector protein from Caulobacter crescentus that is jointly targeted by both signaling molecules, has opened up studies on how these global bacterial networks interact. C-di-GMP and (p)ppGpp compete for the same SmbA binding site, with a dimer of c-di-GMP inducing a conformational change that involves loop 7 of the protein that leads to downstream signaling. Here, we report a crystal structure of a partial loop 7 deletion mutant, SmbA_∆loop in complex with c-di-GMP determined at 1.4 Å resolution. SmbA_∆loop binds monomeric c-di-GMP indicating that loop 7

SUBMITTER: Dubey BN 

PROVIDER: S-EPMC9944927 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature