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TitleCryo-EM structure of the human glucose transporter GLUT7.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 738, Page 150544, Year 2024
Publish dateDec 17, 2024
AuthorsSang Soo Lee / Subin Kim / Mi Sun Jin /
PubMed AbstractGLUT7 is a Class II glucose transporter predominantly expressed at the apical membrane of enterocytes in the small intestine. Here, we report the cryo-EM structure of nanodisc-reconstituted human ...GLUT7 is a Class II glucose transporter predominantly expressed at the apical membrane of enterocytes in the small intestine. Here, we report the cryo-EM structure of nanodisc-reconstituted human GLUT7 in the apo state at 3.3 Å resolution. Our atomic model reveals a typical major facilitator superfamily fold, with the substrate-binding site open to the extracellular side of the membrane. Despite the nearly identical conformation to its closest family member, rat GLUT5, our structure unveils distinct features of the substrate-binding cavity that may influence substrate specificity and binding mode. A homology model of the inward-open human GLUT7 indicates that similar to other members of the GLUT family, it may undergo a global rocker-switch-like reorientation of the transmembrane bundles to facilitate substrate translocation across the membrane. Our work enhances the current structural understanding of the GLUT family, and lays a foundation for rational design of regulators of GLUTs and other sugar transporters.
External linksBiochem Biophys Res Commun / PubMed:39163817
MethodsEM (single particle)
Resolution3.3 Å
Structure data

61099

9j2n

EMDB-61099, PDB-9j2n:
Cryo-EM structure of the human glucose transporter, GLUT7 in outward-facing open conformation
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Human glucose transporter 7 / SLC2A7 / Fructose transporter / Intestinal hexose absorption / Membrane protein

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