Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of human glucose-6-phosphate transporter reveal reciprocal antiport mechanism driving glucose-6-phosphate and inorganic phosphate exchange.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 11441, Year 2025
Publish date	Dec 11, 2025
Authors	Qian Wang / Ningjie Guo / Yunxiang Du / Junwu Liu / Wanting Ai / Fengyi Yang / Yuanzai Zhu / Yuanyuan Zhao / Di Wu / Lei Liu / Xia Yao / Shuai Gao /
PubMed Abstract	Glucose-6-phosphate transporter 1 (G6PT1) is essential for systemic glucose homeostasis, and its deficiency causes glycogen storage disease type 1b (GSD1b). G6PT1 functions as a sugar- ...Glucose-6-phosphate transporter 1 (G6PT1) is essential for systemic glucose homeostasis, and its deficiency causes glycogen storage disease type 1b (GSD1b). G6PT1 functions as a sugar-phosphate/inorganic phosphate (Pi) antiporter, orchestrating G6P transport into the endoplasmic reticulum lumen driven by a Pi gradient. Despite its physiological significance, the molecular mechanisms underlying substrate recognition and antiport activity remain poorly characterized. Here, we present cryo-electron microscopy structures of human G6PT1 in apo, Pi-bound, and GlcN6P-bound (a G6P analogue) states, all captured in cytosol-open conformations. Combined with molecular docking and functional assays, these structures elucidate the molecular basis for Pi and G6P recognition in G6PT1. Comparative analysis reveals that Pi binding triggers an interdomain salt bridge formation, resulting in a thicker luminal gate and a more compact central cavity for G6P binding. In addition to the monomer, we identify a dimeric assembly of G6PT1. Mutating key residues at the dimer interface impairs transport activity, suggesting a regulatory role for oligomerization. Our findings thus provide a mechanistic framework for understanding G6PT1 working mechanism and its pathological dysregulation in GSD1b.
External links	Nat Commun / PubMed:41381426 / PubMed Central
Methods	EM (single particle)
Resolution	2.89 - 3.5 Å
Structure data	64144 9ugu EMDB-64144, PDB-9ugu: Cryo-EM Structure of Apo-G6PT1 Method: EM (single particle) / Resolution: 3.07 Å 64147 9ugx EMDB-64147, PDB-9ugx: Cryo-EM Structure of G6PT1-apo monomer in pi buffer Method: EM (single particle) / Resolution: 3.16 Å 64148 9ugy EMDB-64148, PDB-9ugy: Cryo-EM Structure of G6PT1 bound with GlcN6P Method: EM (single particle) / Resolution: 3.5 Å 66194 9ws8 EMDB-66194, PDB-9ws8: Cryo-EM Structure of G6PT1 treated with G6P Method: EM (single particle) / Resolution: 3.47 Å 66215 9wt2 EMDB-66215, PDB-9wt2: Cryo-EM structure of Pi-free G6PT1 treated with GlcN6P Method: EM (single particle) / Resolution: 3.12 Å 66658 9x8x EMDB-66658, PDB-9x8x: Cryo-EM Structure of G6PT1 bound with lower pi Method: EM (single particle) / Resolution: 2.89 Å 66660 9x95 EMDB-66660, PDB-9x95: Cryo-EM Structure of G6PT1 without GlcN6P Method: EM (single particle) / Resolution: 3.5 Å 66661 9x97 EMDB-66661, PDB-9x97: Cryo-EM Structure of G6PT1 bound with upper pi Method: EM (single particle) / Resolution: 2.89 Å
Chemicals	ChemComp-GLP: 2-amino-2-deoxy-6-O-phosphono-alpha-D-glucopyranose ChemComp-PO4: PHOSPHATE ION
Source	homo sapiens (human)
Keywords	TRANSPORT PROTEIN / G6P