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TitleStructures of human SGLT in the occluded state reveal conformational changes during sugar transport.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2920, Year 2023
Publish dateMay 22, 2023
AuthorsWenhao Cui / Yange Niu / Zejian Sun / Rui Liu / Lei Chen /
PubMed AbstractSodium-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 ...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.
External linksNat Commun / PubMed:37217492 / PubMed Central
MethodsEM (single particle)
Resolution3.26 - 3.48 Å
Structure data

33962

7yni

EMDB-33962, PDB-7yni:
Structure of human SGLT1-MAP17 complex bound with substrate 4D4FDG in the occluded conformation
Method: EM (single particle) / Resolution: 3.26 Å

33963

7ynj

EMDB-33963, PDB-7ynj:
Structure of human SGLT2-MAP17 complex bound with substrate AMG in the occluded conformation
Method: EM (single particle) / Resolution: 3.33 Å

33964

7ynk

EMDB-33964, PDB-7ynk:
Structure of human SGLT2-MAP17 complex in the apo state in the inward-facing conformation
Method: EM (single particle) / Resolution: 3.48 Å

Chemicals

ChemComp-KQC:
(2R,3R,4R,5S,6R)-5-fluoranyl-6-(hydroxymethyl)oxane-2,3,4-triol

ChemComp-GYP:
methyl alpha-D-glucopyranoside

Source
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT / glucose transporter / SGLT / sodium glucose transporter / membrane protein

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