7K5N

Ligand binding domain (tandem PAS/dCache) of Aeromonas caviae diguanylate cyclase with proline bound

7K5N の概要

• エントリーDOI: 10.2210/pdb7k5n/pdb
• 分子名称: Sensor domain-containing diguanylate cyclase, PROLINE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: pas, cache, bacterial inner membrane bound, amino acid binder, signaling protein
• 由来する生物種: Aeromonas caviae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31663.79

構造登録者

Sweeney, E.G.,Remington, S.J. (登録日: 2020-09-17, 公開日: 2021-08-18, 最終更新日: 2023-10-18)

主引用文献

Robinson, C.D.,Sweeney, E.G.,Ngo, J.,Ma, E.,Perkins, A.,Smith, T.J.,Fernandez, N.L.,Waters, C.M.,Remington, S.J.,Bohannan, B.J.M.,Guillemin, K.
Host-emitted amino acid cues regulate bacterial chemokinesis to enhance colonization.
Cell Host Microbe, 29:1221-, 2021

PubMed Abstract: Animal microbiomes are assembled predominantly from environmental microbes, yet the mechanisms by which individual symbionts regulate their transmission into hosts remain underexplored. By tracking the experimental evolution of Aeromonas veronii in gnotobiotic zebrafish, we identify bacterial traits promoting host colonization. Multiple independently evolved isolates with increased immigration harbored mutations in a gene we named sensor of proline diguanylate cyclase enzyme (SpdE) based on structural, biochemical, and phenotypic evidence that SpdE encodes an amino-acid-sensing diguanylate cyclase. SpdE detects free proline and to a lesser extent valine and isoleucine, resulting in reduced production of intracellular c-di-GMP, a second messenger controlling bacterial motility. Indeed, SpdE binding to amino acids increased bacterial motility and host colonization. Hosts serve as sources of SpdE-detected amino acids, with levels varying based on microbial colonization status. Our work demonstrates that bacteria use chemically regulated motility, or chemokinesis, to sense host-emitted cues that trigger active immigration into hosts.

PubMed: 34233153
DOI: 10.1016/j.chom.2021.06.003

実験手法

X-RAY DIFFRACTION (1.8 Å)