8ybq

Choline transporter BetT - CHT bound

spinqualitylabelsall models 8ybq, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ybq is a 3 chain structure with sequence from Pseudomonas syringae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.59Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 Pseudomonas syringae 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 Pseudomonas species, including the plant pathogen P. syringae and the human pathogen Pseudomonas aeruginosa, 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. Structure and mechanism of the osmoregulated choline transporter BetT.,Yang T, Nian Y, Lin H, Li J, Lin X, Li T, Wang R, Wang L, Beattie GA, Zhang J, Fan M Sci Adv. 2024 Aug 16;10(33):eado6229. doi: 10.1126/sciadv.ado6229. Epub 2024 Aug , 14. PMID:39141726 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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