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- Title
Structures of human SGLT in the occluded state reveal conformational changes during sugar transport.
- Authors
Cui, Wenhao; Niu, Yange; Sun, Zejian; Liu, Rui; Chen, Lei
- Abstract
Sodium-Glucose Cotransporters (SGLT) mediate the uphill uptake of extracellular sugars and play fundamental roles in sugar metabolism. Although their structures in inward-open and outward-open conformations are emerging from structural studies, the trajectory of how SGLTs transit from the outward-facing to the inward-facing conformation remains unknown. Here, we present the cryo-EM structures of human SGLT1 and SGLT2 in the substrate-bound state. Both structures show an occluded conformation, with not only the extracellular gate but also the intracellular gate tightly sealed. The sugar substrate are caged inside a cavity surrounded by TM1, TM2, TM3, TM6, TM7, and TM10. Further structural analysis reveals the conformational changes associated with the binding and release of substrates. These structures fill a gap in our understanding of the structural mechanisms of SGLT transporters. SGLT plays key roles in sugar uptake and reabsorption. Here the authors provided the cryo-EM structures of human SGLT1 and SGLT2 in the substrate-bound occluded state, uncovering the conformational changes of SGLT during sugar transport.
- Subjects
CONFORMATIONAL analysis; SODIUM-glucose cotransporters; SUGAR; SUGARS; LACTOGLOBULINS
- Publication
Nature Communications, 2023, Vol 14, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-023-38720-1