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<p>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.</p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年10月27日

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  • Christian Tüting,
  • Kevin Janson,
  • Michelle Kammel,
  • Christian Ihling,
  • Jana Lorenz,
  • Fotis L. Kyrilis,
  • Farzad Hamdi,
  • Christopher Erdmann,
  • Andrea Sinz,
  • R. Gary Sawers,
  • Panagiotis L. Kastritis

摘要

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.