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Updated: Sep 9, 2025

Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles
Published on: December 31, 2019
Structural basis of a GatC ortholog transporter in the bacterial phosphotransferase system
Yutaro S Takahashi1, Hidetaka Kohga1, Min Fey Chek1,2
1Graduate School of Science and Technology, Nara Institute of Science and Technology, Japan.
Abstract:
The bacterial phosphotransferase system (PTS) mediates the uptake of specific carbohydrates via IIC transporters. Here, we report the crystal and cryo-electron microscopy (cryo-EM) structures of Leminorella grimontii galactitol-specific PTS enzyme IIC component (LgGatC), which is implicated in D-xylose uptake and belongs to the ascorbate-galactitol (AG) superfamily of IIC proteins. These structures, determined in the presence and absence of D-xylose, capture the transporter in an outward-facing conformation. A homology model of an inward-facing state, constructed based on these structures, supports an elevator-like transport mechanism. These findings provide structural insights into substrate recognition by GatC and offer a framework for understanding sugar transport in PTS IIC proteins.
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