Structures of human SGLT in the occluded state reveal conformational changes during sugar transport

Wenhao Cui, Yange Niu, Zejian Sun, Rui Liu and Lei Chen ()
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Wenhao Cui: Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Yange Niu: Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Zejian Sun: Peking University
Rui Liu: Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Lei Chen: Beijing Key Laboratory of Cardiometabolic Molecular Medicine

Nature Communications, 2023, vol. 14, issue 1, 1-10

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-38720-1

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