9G49

Cryo-EM reconstruction of the full-length E. coli transmembrane formate transporter FocA

9G49 の概要

• エントリーDOI: 10.2210/pdb9g49/pdb
• EMDBエントリー: 51034
• 分子名称: Formate channel FocA (2 entities in total)
• 機能のキーワード: fnt-transporter, foca, formate, membrane protein
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31012.60

構造登録者

Tueting, C.,Janson, K.,Kyrilis, F.L.,Hamdi, F.,Kastritis, P.L. (登録日: 2024-07-15, 公開日: 2025-10-22, 最終更新日: 2025-11-05)

主引用文献

Tuting, C.,Janson, K.,Kammel, M.,Ihling, C.,Lorenz, J.,Kyrilis, F.L.,Hamdi, F.,Erdmann, C.,Sinz, A.,Sawers, R.G.,Kastritis, P.L.
Conserved hydrophilic checkpoints tune FocA-mediated formate:H + symport.
Nat Commun, 16:9476-9476, 2025

PubMed 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.

PubMed: 41145500
DOI: 10.1038/s41467-025-65159-3

実験手法

ELECTRON MICROSCOPY (2.56 Å)