Proteomics

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Conserved hydrophilic checkpoints tune FocA-1 mediated formate:H+ symport

ABSTRACT: FocA belongs to the widespread, evolutionarily ancient formate-nitrite transporter 30 (FNT) family of pentameric anion channels and translocates formic acid bidirectionally. 31 Here, we identify compartmentalized polarity distribution across the complete FocA 32 pore structure – resolved at 2.56 Å – mirrored against a two-fold axis with H209 at its 33 center. The FocA-H209N efflux-only variant reveals a density consistent with formic 34 acid located directly at N209, breaking local polarity distribution. Pyruvate formate-35 lyase, generating formate, orients at the cytoplasmic face where formate delivery is 36 regulated by conformational changes in the FocA vestibule. Comparisons with other 37 FNTs suggest a tuning mechanism of formate-specific transport via checkpoints 38 enriched in hydrophilic residues.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli

SUBMITTER: Christian Ihling  

LAB HEAD: R. Gary Sawers

PROVIDER: PXD054538 | Pride | 2025-11-10

REPOSITORIES: Pride

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Dataset's files

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Action DRS
Pep_PflB_Urea_1mM.mgf Mgf
Pep_PflB_Urea_1mM.raw Raw
Pep_PflB_Urea_1mM.zhrm Other
Pep_Pflb_Urea_05mM.mgf Mgf
Pep_Pflb_Urea_05mM.raw Raw
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Publications

Conserved hydrophilic checkpoints tune FocA-mediated formate:H<sup>+</sup> symport.

Tüting Christian C   Janson Kevin K   Kammel Michelle M   Ihling Christian C   Lorenz Jana J   Kyrilis Fotis L FL   Hamdi Farzad F   Erdmann Christopher C   Sinz Andrea A   Sawers R Gary RG   Kastritis Panagiotis L PL  

Nature communications 20251027 1

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, ab  ...[more]

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