8YBQ

Choline transporter BetT - CHT bound

8YBQ の概要

• エントリーDOI: 10.2210/pdb8ybq/pdb
• EMDBエントリー: 39121
• 分子名称: BCCT family transporter, CHOLINE ION (3 entities in total)
• 機能のキーワード: choline transporter, choline-binding protein
• 由来する生物種: Pseudomonas syringae
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 226076.55

構造登録者

Yang, T.J.,Nian, Y.W.,Lin, H.J.,Li, J.,Zhang, J.R.,Fan, M.R. (登録日: 2024-02-16, 公開日: 2024-09-04, 最終更新日: 2025-06-18)

主引用文献

Yang, T.,Nian, Y.,Lin, H.,Li, J.,Lin, X.,Li, T.,Wang, R.,Wang, L.,Beattie, G.A.,Zhang, J.,Fan, M.
Structure and mechanism of the osmoregulated choline transporter BetT.
Sci Adv, 10:eado6229-eado6229, 2024

PubMed Abstract: The choline-glycine betaine pathway plays an important role in bacterial survival in hyperosmotic environments. Osmotic activation of the choline transporter BetT promotes the uptake of external choline for synthesizing the osmoprotective glycine betaine. Here, we report the cryo-electron microscopy structures of BetT in the apo and choline-bound states. Our structure shows that BetT forms a domain-swapped trimer with the C-terminal domain (CTD) of one protomer interacting with the transmembrane domain (TMD) of a neighboring protomer. The substrate choline is bound within a tryptophan prism at the central part of TMD. Together with functional characterization, our results suggest that in species, including the plant pathogen and the human pathogen , BetT is locked at a low-activity state through CTD-mediated autoinhibition in the absence of osmotic stress, and its hyperosmotic activation involves the release of this autoinhibition.

PubMed: 39141726
DOI: 10.1126/sciadv.ado6229

実験手法

ELECTRON MICROSCOPY (2.59 Å)