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Molecular determinants of permeation in a fluoride-specific ion channel
Abstract
Fluoride ion channels of the Fluc family combat toxicity arising from accumulation of environmental F-. Although crystal structures are known, the densely packed pore region has precluded delineation of the ion pathway. Here we chart out the Fluc pore and characterize its chemical requirements for transport. A ladder of H-bond donating residues creates a ‘polar track’ demarking the ion-conduction pathway. Surprisingly, while track polarity is well conserved, polarity is nonetheless functionally dispensable at several positions. A threonine at one end of the pore engages in vital interactions through its β-branched methyl group. Two critical central phenylalanines that directly coordinate F- through a quadrupolar-ion interaction cannot be functionally substituted by aromatic, non-polar, or polar sidechains. The only functional replacement is methionine, which coordinates F- through its partially positive γ-methylene in mimicry of phenylalanine’s quadrupolar interaction. These results demonstrate the unusual chemical requirements for selectively transporting the strongly H-bonding F- anion.
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The polar track residues are somewhat more tolerant of alanine substitution than the sidechains that coordinate F0.
“Alteration of N43 typically eliminates fluoride transport entirely (73, 85); the polar track residues, like the sidechains that coordinate F0, are somewhat more tolerant of alanine substitution(85).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [85]
In a handful of bacterial Fluc homologues, the phenylalanine box sequence motif includes a methionine instead.
“This interaction calls to mind the CLCF’s coordination of Fcen by a methionine, and in a handful of bacterial Fluc homologues, the phenylalanine box sequence motif includes a methionine instead(85).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [85]
Alteration of N43 typically eliminates fluoride transport entirely.
“Alteration of N43 typically eliminates fluoride transport entirely (73, 85); the polar track residues, like the sidechains that coordinate F0, are somewhat more tolerant of alanine substitution(85).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [85]
Mutation of F82 or F85 to methionine supports fluoride conductance at wildtype levels.
“However, mutation to methionine, which is, like phenylalanine, both hydrophobic and polarizable, supports fluoride conductance at wildtype levels (85).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [85]
Mutation of F82 or F85 to polar aromatic sidechains like tyrosine and tryptophan does not support transport.
“Mutation to polar aromatic sidechains like tyrosine and tryptophan do not support transport either(85).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [85]
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Cites
Crystal structures of a double-barrelled fluoride ion channel
Stockbridge, R. B., Kolmakova-Partensky, L., Shane, T., Koide, A., Koide, S., Miller, C., & Newstead, S. (2015) · Nature · doi:10.1038/nature14981 · Cited by 119
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Cited by
Sorted by citations
Membrane exporters of fluoride ion
McIlwain, B. C., Ruprecht, M. T., & Stockbridge, R. B. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071520-112507 · Cited by 69
Hu, M., & Scott, C. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.00157-24 · Cited by 63
Metadata
- Authors
- Last, N. B., Sun, S., Pham, M. C., & Miller, C.
- Affiliations
- Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, United States
- ORCID
- Miller, Christopher
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2017-09-27
- Volume
- 6
- ISSN
- 2050-084X
- PMC
- PMC5636608
- Cited by
- 25
- References
- 1
- Language
- en
- Licence
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (NIH GM107023)
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