August 5, 2025FEBS Letters

Structural basis of a GatC ortholog transporter in the bacterial phosphotransferase system

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Discussion

Crystal and cryo-EM structures reveal D-xylose dynamics in Leminorella grimontii transporter, suggesting a mechanism for sugar transport.

The study identifies the crystal and cryo-EM structures of the LgGatC transporter, revealing its outward-facing conformation.
Findings imply D-xylose binding alters the transporter's conformation during sugar uptake.
A homology model supports an elevator-like mechanism for substrate transport in IIC proteins.
This work clarifies how GatC recognizes substrates, contributing to the understanding of carbohydrate uptake in bacteria.

Takahashi et al. (2025) studied this question.

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