Structure-function studies of Vibrio cholerae quorum-sensing receptor CqsR signal recognition.

ABSTRACT: Ethanolamine signaling through the transmembrane quorum-sensing receptor CqsR influences Vibrio cholerae niche recognition and host colonization. In this study, we present a comprehensive structure-function analysis of CqsR. Specifically, we have determined X-ray crystal structures of the CqsR periplasmic domain bound to the signaling agonist ethanolamine and its analogs, serinol and L-alaninol, as well as the ligand-free (apo) form of CqsR. The periplasmic ligand-binding domain of CqsR is a Cache domain, the most prevalent extracellular sensory module in prokaryotes. Our findings provide a rare structural comparison of ligand-bound and unbound states of a Cache domain receptor. Coupled with thermodynamic binding assays and genetic analyses, these structures elucidate the molecular basis o

SUBMITTER: Guarnaccia AM 

PROVIDER: S-EPMC12410723 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature