8YBQ
Choline transporter BetT - CHT bound
Summary for 8YBQ
| Entry DOI | 10.2210/pdb8ybq/pdb |
| EMDB information | 39121 |
| Descriptor | BCCT family transporter, CHOLINE ION (3 entities in total) |
| Functional Keywords | choline transporter, choline-binding protein |
| Biological source | Pseudomonas syringae |
| Total number of polymer chains | 3 |
| Total formula weight | 226076.55 |
| Authors | Yang, T.J.,Nian, Y.W.,Lin, H.J.,Li, J.,Zhang, J.R.,Fan, M.R. (deposition date: 2024-02-16, release date: 2024-09-04) |
| Primary citation | 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 Cited by 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: 39141726DOI: 10.1126/sciadv.ado6229 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.59 Å) |
Structure validation
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