Structure and mechanism of a phosphotransferase system glucose transporter.

Autor: Roth P; Institute of Biochemistry and Molecular Medicine, Medical Faculty, University of Bern, Bern, Switzerland., Jeckelmann JM; Institute of Biochemistry and Molecular Medicine, Medical Faculty, University of Bern, Bern, Switzerland., Fender I; Institute of Biochemistry and Molecular Medicine, Medical Faculty, University of Bern, Bern, Switzerland., Ucurum Z; Institute of Biochemistry and Molecular Medicine, Medical Faculty, University of Bern, Bern, Switzerland., Lemmin T; Institute of Biochemistry and Molecular Medicine, Medical Faculty, University of Bern, Bern, Switzerland., Fotiadis D; Institute of Biochemistry and Molecular Medicine, Medical Faculty, University of Bern, Bern, Switzerland. dimitrios.fotiadis@unibe.ch.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2024 Sep 12; Vol. 15 (1), pp. 7992. Date of Electronic Publication: 2024 Sep 12.
DOI: 10.1038/s41467-024-52100-3
Abstrakt: 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 Glc 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 Glc 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 Glc transporter in a native-like lipid environment.
(© 2024. The Author(s).)
Databáze: MEDLINE
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