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TitleMechanism of substrate recognition and release of human SGLT2.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 7140, Year 2025
Publish dateAug 4, 2025
AuthorsWenhao Cui / Zejian Sun / Jiaxuan Xu / Xiaoyu Liu / Yunlu Kang / Lei Chen /
PubMed AbstractGlucose is a vital energy source essential for life and human health. Sodium-glucose cotransporter 2 (SGLT2) is a sodium-glucose symporter that utilizes the electrochemical gradient of sodium to ...Glucose is a vital energy source essential for life and human health. Sodium-glucose cotransporter 2 (SGLT2) is a sodium-glucose symporter that utilizes the electrochemical gradient of sodium to reabsorb glucose from kidney filtrate back into circulation. SGLT2 plays a crucial role in maintaining blood glucose homeostasis and is an important drug target for type 2 diabetes. Despite its significance, the mechanisms by which SGLT2 recognizes and releases substrates during its transport cycle remain largely unknown. Here, we present structures of human SGLT2 in complex with a glucose analogue in the occluded conformation at 2.6 Å resolution, revealing a detailed hydrogen bonding network at the substrate binding site that governs substrate recognition. Additionally, structures of SGLT2 in both the substrate-bound inward-facing conformation and the substrate-free inward-facing conformations illustrate the structural changes that occur during substrate release into cytosol. Our structural analysis, combined with mutagenesis results, identifies specific polar interactions that are essential for maintaining the outer and inner gates in their closed conformations.
External linksNat Commun / PubMed:40759649 / PubMed Central
MethodsEM (single particle)
Resolution2.47 - 3.16 Å
Structure data

62395

9kkq

EMDB-62395, PDB-9kkq:
Structure of hSGLT2-MAP17 complex in the substrate-bound occluded conformation
Method: EM (single particle) / Resolution: 2.6 Å

62396

9kkw

EMDB-62396, PDB-9kkw:
Structure of hSGLT2-MAP17 complex in the substrate-free inward-facing conformation in the presence of sodium
Method: EM (single particle) / Resolution: 2.92 Å

62398

9kl0

EMDB-62398, PDB-9kl0:
Structure of hSGLT2-MAP17 complex in the substrate-free inward-facing conformation in the presence of potassium
Method: EM (single particle) / Resolution: 3.16 Å

62439

9kmn

EMDB-62439, PDB-9kmn:
Structure of hSGLT2-MAP17 complex in the substrate-bound inward-facing conformation
Method: EM (single particle) / Resolution: 2.47 Å

Chemicals

ChemComp-NA:
Unknown entry

PDB-1efw:
Crystal structure of aspartyl-tRNA synthetase from Thermus thermophilus complexed to tRNAasp from Escherichia coli

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / glucose transporter / SGLT / sodium glucose transporter / membrane protein

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