Structure and mechanism of a phosphotransferase system glucose transporter

Patrick Roth, Jean-Marc Jeckelmann, Inken Fender, Zöhre Ucurum, Thomas Lemmin and Dimitrios Fotiadis ()
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Patrick Roth: University of Bern
Jean-Marc Jeckelmann: University of Bern
Inken Fender: University of Bern
Zöhre Ucurum: University of Bern
Thomas Lemmin: University of Bern
Dimitrios Fotiadis: University of Bern

Nature Communications, 2024, vol. 15, issue 1, 1-10

Abstract: 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 IICBGlc 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 IICBGlc 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 IICBGlc transporter in a native-like lipid environment.

Date: 2024
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DOI: 10.1038/s41467-024-52100-3

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