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TitleStructure and mechanism of a phosphotransferase system glucose transporter.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 7992, Year 2024
Publish dateSep 12, 2024
AuthorsPatrick Roth / Jean-Marc Jeckelmann / Inken Fender / Zöhre Ucurum / Thomas Lemmin / Dimitrios Fotiadis /
PubMed AbstractGlucose 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 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.
External linksNat Commun / PubMed:39266522 / PubMed Central
MethodsEM (single particle)
Resolution2.56 - 2.89 Å
Structure data

18640

8qsr

EMDB-18640: Cryo-EM structure of the glucose-specific PTS transporter IICB from E. coli in the inward-open state
PDB-8qsr: Cryo-EM structure of the glucose-specific PTS transporter IICB from E. coli in the inward-facing conformation
Method: EM (single particle) / Resolution: 2.56 Å

18641

8qst

EMDB-18641: Cryo-EM structure of the glucose-specific PTS transporter IICB from E. coli in the inward-open state
PDB-8qst: Cryo-EM structure of the glucose-specific PTS transporter IICB from E. coli in the inward- and outward-facing conformation
Method: EM (single particle) / Resolution: 2.89 Å

Chemicals

ChemComp-BGC:
beta-D-glucopyranose

Source
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / glucose transport protein / membrane protein

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