4LDS
The inward-facing structure of the glucose transporter from Staphylococcus epidermidis
Summary for 4LDS
| Entry DOI | 10.2210/pdb4lds/pdb |
| Descriptor | Glucose transporter GlcP (1 entity in total) |
| Functional Keywords | alpha helical transmembrane protein, glucose transporter, major facilitator superfamily, transport protein, membrane protein |
| Biological source | Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) |
| Total number of polymer chains | 2 |
| Total formula weight | 96814.95 |
| Authors | Choe, J.,Aleshin, A.,Iancu, C.V. (deposition date: 2013-06-25, release date: 2013-10-16, Last modification date: 2024-02-28) |
| Primary citation | Iancu, C.V.,Zamoon, J.,Woo, S.B.,Aleshin, A.,Choe, J.Y. Crystal structure of a glucose/H+ symporter and its mechanism of action. Proc.Natl.Acad.Sci.USA, 110:17862-17867, 2013 Cited by PubMed Abstract: Glucose transporters are required to bring glucose into cells, where it is an essential energy source and precursor in protein and lipid synthesis. These transporters are involved in important common diseases such as cancer and diabetes. Here, we report the crystal structure of the Staphylococcus epidermidis glucose/H(+) symporter in an inward-facing conformation at 3.2-Å resolution. The Staphylococcus epidermidis glucose/H(+) symporter is homologous to human glucose transporters, is very specific and has high avidity for glucose, and is inhibited by the human glucose transport inhibitors cytochalasin B, phloretin, and forskolin. On the basis of the crystal structure in conjunction with mutagenesis and functional studies, we propose a mechanism for glucose/H(+) symport and discuss the symport mechanism versus facilitated diffusion. PubMed: 24127585DOI: 10.1073/pnas.1311485110 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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