9U84

Cryo-EM structure of Leminorella grimontii GatC in the absence of D-xylose

Summary for 9U84

• Entry DOI: 10.2210/pdb9u84/pdb
• EMDB information: 63951
• Descriptor: PTS galactitol transporter subunit IIC (1 entity in total)
• Functional Keywords: pts, xylose, transporter, transport protein
• Biological source: Leminorella grimontii
• Total number of polymer chains: 2
• Total formula weight: 100156.12

Authors

Takahashi, Y.S.,Kohaga, H.,Shigematsu, H.,Miyazaki, R.,Tsukazaki, T. (deposition date: 2025-03-25, release date: 2025-10-15, Last modification date: 2026-03-04)

Primary citation

Takahashi, Y.S.,Kohga, H.,Chek, M.F.,Yamamoto, K.,Takahashi, J.F.,Shigematsu, H.,Tanaka, Y.,Ichikawa, M.,Miyazaki, R.,Hakoshima, T.,Tsukazaki, T.
Structural basis of a GatC ortholog transporter in the bacterial phosphotransferase system.
Febs Lett., 599:2377-2387, 2025

PubMed 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.

PubMed: 40878824
DOI: 10.1002/1873-3468.70135

Experimental method

ELECTRON MICROSCOPY (3.27 Å)