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TitleStructural basis for transport and inhibition of the human glucose-6-phosphate transporter G6PT.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 9420, Year 2025
Publish dateOct 24, 2025
AuthorsZhanyi Xia / Yaqi Wang / Di Wu / Cheng Chi / Chen Li / Ligong Chen / Daohua Jiang /
PubMed AbstractThe human glucose-6-phosphate transporter (G6PT) moves glucose-6-phosphate (G6P) into the lumen of endoplasmic reticulum, playing a vital role in glucose homeostasis. Dysregulation of G6PT causes ...The human glucose-6-phosphate transporter (G6PT) moves glucose-6-phosphate (G6P) into the lumen of endoplasmic reticulum, playing a vital role in glucose homeostasis. Dysregulation of G6PT causes glycogen storage disease 1b. Despite its functional importance, the structure, G6P recognition, and inhibition mechanism of G6PT remain unclear. Here, we report the cryo-EM structures of human G6PT in apo, G6P-bound, and the specific inhibitor chlorogenic acid (CHA)-bound forms, elucidating the structural basis for G6PT transport and inhibition. The G6P pocket comprises subsite A for phosphate and subsite B for glucose. The CHA occupies the G6P site and locks G6PT in a partly-occluded state. Functional assays demonstrate that G6PT activity is enhanced by co-expression of glucose-6-phosphatase (G6PC), but G6PT does not form a complex with G6PC. Together, this study provides a solid foundation for understanding the structure‒function relationships and pathology of G6PT and sheds light on the future development of potential therapeutics targeting G6PT.
External linksNat Commun / PubMed:41136424 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 3.6 Å
Structure data

62584

9kuy

EMDB-62584, PDB-9kuy:
Cryo-EM structure of human G6PT in apo state
Method: EM (single particle) / Resolution: 3.6 Å

62585

9kv0

EMDB-62585, PDB-9kv0:
Cryo-EM structure of human G6PT in complex with chlorogenic acid
Method: EM (single particle) / Resolution: 3.4 Å

62602

9kvv

EMDB-62602, PDB-9kvv:
Cryo-EM structure of human G6PT in complex with G6P
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

PDB-1eg7:
THE CRYSTAL STRUCTURE OF FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA

ChemComp-BG6:
6-O-phosphono-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / G6PT / cryo-EM / apo / chlorogenic acid / G6P

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