9NIT

Crystal structure of Vibrio cholerae CqsR bound to L-alaninol

9NIT の概要

• エントリーDOI: 10.2210/pdb9nit/pdb
• 関連するPDBエントリー: 9NIA
• 分子名称: histidine kinase, (2S)-2-aminopropan-1-ol, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: quorum-sensing receptor, double cache domain, periplasmic ligand-binding receptor, 2-amino alcohol receptor, signaling protein
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24317.34

構造登録者

Guarnaccia, A.M.,Neiditch, M.B. (登録日: 2025-02-26, 公開日: 2025-07-02, 最終更新日: 2025-09-17)

主引用文献

Guarnaccia, A.M.,Steenhaut, A.D.,Olenic, S.D.,Na, J.,Perez, L.J.,Ng, W.L.,Neiditch, M.B.
Structure-function studies of Vibrio cholerae quorum-sensing receptor CqsR signal recognition.
Plos Pathog., 21:e1013447-e1013447, 2025

PubMed 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 of CqsR ligand specificity. This study not only advances the understanding of Cache domain function but also informs the identification of ligands for orphan Cache receptors and the rational design of signaling agonists and antagonists. Lastly, we discuss ligand-induced conformational changes in the CqsR Cache domains and explore the potential for the existence of additional regulatory ligands.

PubMed: 40906767
DOI: 10.1371/journal.ppat.1013447

実験手法

X-RAY DIFFRACTION (1.72 Å)