9J2N
Cryo-EM structure of the human glucose transporter, GLUT7 in outward-facing open conformation
Summary for 9J2N
| Entry DOI | 10.2210/pdb9j2n/pdb |
| EMDB information | 61099 |
| Descriptor | Solute carrier family 2, facilitated glucose transporter member 7, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | human glucose transporter 7, slc2a7, fructose transporter, intestinal hexose absorption, membrane protein, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 55998.40 |
| Authors | |
| Primary citation | Lee, S.S.,Kim, S.,Jin, M.S. Cryo-EM structure of the human glucose transporter GLUT7. Biochem.Biophys.Res.Commun., 738:150544-150544, 2024 Cited by PubMed Abstract: 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. PubMed: 39163817DOI: 10.1016/j.bbrc.2024.150544 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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