8QSR
Cryo-EM structure of the glucose-specific PTS transporter IICB from E. coli in the inward-facing conformation
Summary for 8QSR
| Entry DOI | 10.2210/pdb8qsr/pdb |
| EMDB information | 18640 |
| Descriptor | PTS system glucose-specific EIICB component, beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | glucose transport protein, membrane protein, transport protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 107242.67 |
| Authors | Roth, P.,Fotiadis, D.,Jeckelmann, J.-M. (deposition date: 2023-10-11, release date: 2024-09-25, Last modification date: 2025-01-22) |
| Primary citation | Roth, P.,Jeckelmann, J.M.,Fender, I.,Ucurum, Z.,Lemmin, T.,Fotiadis, D. Structure and mechanism of a phosphotransferase system glucose transporter. Nat Commun, 15:7992-7992, 2024 Cited by PubMed Abstract: Glucose is the primary source of energy for many organisms and is efficiently taken up by bacteria through a dedicated transport system that exhibits high specificity. In Escherichia coli, the glucose-specific transporter IICB serves as the major glucose transporter and functions as a component of the phosphoenolpyruvate-dependent phosphotransferase system. Here, we report cryo-electron microscopy (cryo-EM) structures of the glucose-bound IICB protein. The dimeric transporter embedded in lipid nanodiscs was captured in the occluded, inward- and occluded, outward-facing conformations. Together with biochemical and biophysical analyses, and molecular dynamics (MD) simulations, we provide insights into the molecular basis and dynamics for substrate recognition and binding, including the gates regulating the binding sites and their accessibility. By combination of these findings, we present a mechanism for glucose transport across the plasma membrane. Overall, this work provides molecular insights into the structure, dynamics, and mechanism of the IICB transporter in a native-like lipid environment. PubMed: 39266522DOI: 10.1038/s41467-024-52100-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.56 Å) |
Structure validation
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