Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410

Remm, Sille; De Vecchis, Dario; Schöppe, Jendrik; Hutter, Cedric A J; Gonda, Imre; Hohl, Michael; Newstead, Simon; Schäfer, Lars V; Seeger, Markus A

doi:10.1038/s41467-023-42073-0

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Remm, S., De Vecchis, D., Schöppe, J., Hutter, C. A. J., Gonda, I., Hohl, M., Newstead, S., Schäfer, L. V., & Seeger, M. A. (2023). Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410. Nature Communications, 14(1), 6449. https://doi.org/10.1038/s41467-023-42073-0

Abstract

Mycobacterium tuberculosis is protected from antibiotic therapy by a multi-layered hydrophobic cell envelope. Major facilitator superfamily (MFS) transporter Rv1410 and the periplasmic lipoprotein LprG are involved in transport of triacylglycerides (TAGs) that seal the mycomembrane. Here, we report a 2.7 Å structure of a mycobacterial Rv1410 homologue, which adopts an outward-facing conformation and exhibits unusual transmembrane helix 11 and 12 extensions that protrude ~20 Å into the periplasm. A small, very hydrophobic cavity suitab