Structural basis of a <scp>GatC</scp> ortholog transporter in the bacterial phosphotransferase system

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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Publication Details

Journal
FEBS Letters
Published
2025-08-01
DOI
https://doi.org/10.1002/1873-3468.70135
Citations
1
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
1.82

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article

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

Muneyoshi Ichikawa, Tomoya Tsukazaki, Yoshiki Tanaka, Toshio Hakoshima et al.
1 citations
FEBS Letters
Bacterial Genetics and Biotechnology
1.82
article

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

Muneyoshi Ichikawa, Tomoya Tsukazaki, Yoshiki Tanaka, Toshio Hakoshima, Hideki Shigematsu, Keiko Yamamoto, J Takahashi, Hidetaka Kohga, Ryoji Miyazaki, Min Fey Chek, Yutaro S. Takahashi
article en
1 citations

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.

FEBS LettersVol. 599(16)
Fudan University (CN), Japan Synchrotron Radiation Research Institute (JP), Nara Institute of Science and Technology (JP)
Natural Science Foundation of Shanghai, Takeda Science Foundation
Openalex Percentile: Top 14%
Bacterial Genetics and Biotechnology
1.82
DOISourceOpenAlex
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Structural basis of a <scp>GatC</scp> ortholog transporter in the bacterial phosphotransferase system — Muneyoshi Ichikawa, Tomoya Tsukazaki, et al. · FEBS Letters (2025) | TGRS Research Map | TGRS