Conserved hydrophilic checkpoints tune FocA-mediated formate:H+ symport

Christian Tüting, Kevin Janson, Michelle Kammel, Christian Ihling, Jana Lorenz, Fotis L. Kyrilis, Farzad Hamdi, Christopher Erdmann, Andrea Sinz, R. Gary Sawers () and Panagiotis L. Kastritis ()
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Christian Tüting: Kurt-Mothes-Straße 3a
Kevin Janson: Kurt-Mothes-Straße 3a
Michelle Kammel: Kurt-Mothes-Str. 3
Christian Ihling: Kurt-Mothes-Str. 3
Jana Lorenz: Kurt-Mothes-Str. 3
Fotis L. Kyrilis: Kurt-Mothes-Straße 3a
Farzad Hamdi: Kurt-Mothes-Straße 3a
Christopher Erdmann: Kurt-Mothes-Str. 3
Andrea Sinz: Kurt-Mothes-Str. 3
R. Gary Sawers: Kurt-Mothes-Str. 3
Panagiotis L. Kastritis: Kurt-Mothes-Straße 3a

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: Abstract FocA belongs to the widespread, evolutionarily ancient formate-nitrite transporter (FNT) family of pentameric anion channels and translocates formic acid bidirectionally. Here, we identify compartmentalized polarity distribution across the complete FocA pore structure – resolved at 2.56 Å – mirrored against a two-fold axis with H209 at its center. A FocA-H209N variant that exhibits an efflux-only channel-like function in vivo reveals a density consistent with formate located directly at N209, abolishing the channel’s amphiphilicity. Pyruvate formate-lyase, which generates formate, orients at the cytoplasmic face where formate delivery is regulated by conformational changes in the FocA vestibule. Comparisons with other FNTs suggest a tuning mechanism of formate-specific transport via checkpoints enriched in hydrophilic residues.

Date: 2025
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DOI: 10.1038/s41467-025-65159-3

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