7YNI

Structure of human SGLT1-MAP17 complex bound with substrate 4D4FDG in the occluded conformation

Summary for 7YNI

• Entry DOI: 10.2210/pdb7yni/pdb
• EMDB information: 33962
• Descriptor: Sodium/glucose cotransporter 1, PDZK1-interacting protein 1, (2R,3R,4R,5S,6R)-5-fluoranyl-6-(hydroxymethyl)oxane-2,3,4-triol (3 entities in total)
• Functional Keywords: glucose transporter, sglt, sodium glucose transporter, membrane protein, protein transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 85974.85

Authors

Chen, L.,Niu, Y.,Cui, W. (deposition date: 2022-07-31, release date: 2023-05-31, Last modification date: 2024-11-13)

Primary citation

Cui, W.,Niu, Y.,Sun, Z.,Liu, R.,Chen, L.
Structures of human SGLT in the occluded state reveal conformational changes during sugar transport.
Nat Commun, 14:2920-2920, 2023

PubMed 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.

PubMed: 37217492
DOI: 10.1038/s41467-023-38720-1

Experimental method

ELECTRON MICROSCOPY (3.26 Å)