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Proof of dual-topology architecture of Fluc F− channels with monobody blockers
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Fluc proteins are small, homodimeric permeases, with extremely high specificity for fluoride anion (10,000-fold versus chloride).
“The Fluc proteins are small, homodimeric permeases (175), with extremely high specificity for the fluoride anion (10,000-fold versus chloride) (176).”
From Toward the development of a molecular toolkit for the microbial remediation of per-and polyfluoroalkyl substances (2024) · cites this paper as [176]
Proteins encoded by the crcB genes are electrodiffusive F− channels.
“Electrophysiological characterization showed that the proteins encoded by the crcB genes are electrodiffusive F− channels (2, 3, 60–63), and they were renamed Fluc (Fluoride channel) in bacteria and FEX (Fluoride exporter) in eukaryotes.”
From Membrane exporters of fluoride ion (2021) · cites this paper as [60]
An inhibitor applied in sequence to the cis and trans sides of a single Fluc channel in a planar lipid bilayer blocks both sides of the channel with identical kinetics.
“Functional experiments support this observation: an inhibitor applied in sequence to the cis and trans sides of a single Fluc channel in a planar lipid bilayer blocks both sides of the channel with identical kinetics (60–62).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [60]
Bacterial Flucs assemble as dual topology dimers, with one subunit inserted into the membrane with the termini facing out, and the other inserted with the termini facing in.
“Remarkably, the bacterial Flucs embody this evolutionary antecedent, assembling as dual topology dimers, with one subunit inserted into the membrane with the termini facing out, and the other inserted into the membrane with the termini facing in (2, 60).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [60]
Synthetic proteins that inhibit fluoride channels have been developed but have not been tested in biological systems, and no such natural regulatory mechanism has been identified.
“Although synthetic proteins that inhibit fluoride channels have been developed123–125, they have not been tested in biological systems, and no such natural regulatory mechanism has been identified.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [123]
Fluc channels exhibit extreme selectivity for F- over Cl- and dual-topology dimeric assembly.
“including extreme selectivity for F- over Cl- and dual-topology dimeric assembly5–6.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [6]
Ec2 is a homologue of only 33% identity, shows similar electrophysiological behavior to Bpe, and is blocked by S9 at nanomolar concentrations.
“This homologue of only 33% identity shows similar electrophysiological behavior to Bpe and is blocked by S9 at nanomolar concentrations6.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [6]
Fluc proteins are ion channels with high specificity (>10^4) for F- over Cl- and a dual-topology dimeric architecture.
“We recently established5,6 that Fluc proteins are ion channels with two unusual properties: an exceedingly high specificity (>104) for F- over Cl–, and a dual-topology dimeric architecture”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [6]
The antiparallel transmembrane topology of Fluc channels was established definitively by two-sided block of single channels by monobodies.
“was established definitively by two-sided block of single channels by “monobodies,” engineered proteins selected as high-affinity binding partners from combinatorial libraries6.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [6]
Diffraction to 3.6 Å Bragg spacing was obtained with monobody Mb(Bpe-S7).
“however diffraction to 3.6 Å Bragg spacing was obtained with monobody Mb(Bpe-S7)6, hereafter denoted S7.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [6]
The structures represent the monobody-blocked state similar to that observed electrophysiologically.
“The structures here would represent the monobody-blocked state similar to that observed electrophysiologically6,15.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [6]
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Citations
Cites
Nanobody stabilization of G protein-coupled receptor conformational states
Steyaert, J., & Kobilka, B. K. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.06.011 · Cited by 234
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- Nasie, I., Steiner-Mordoch, S., Gold, A. & Schuldiner, S. Topologically random insertion of EmrE supports a pathway for evolution of inverted repeats in ion-coupled transporters. J. Biol. Chem. 285, 15234–15244 (2010). · DOI
- Morrison, E. A. et al. Antiparallel EmrE exports drugs by exchanging between asymmetric structures. Nature 481, 45–50 (2012). · DOI · Paper page
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- Koide, A., Wojcik, J., Gilbreth, R. N., Hoey, R. J. & Koide, S. Teaching an old scaffold new tricks: monobodies constructed using alternative surfaces of the FN3 scaffold. J. Mol. Biol. 415, 393–405 (2012). · DOI · Paper page
- Heginbotham, L., LeMasurier, M., Kolmakova-Partensky, L. & Miller, C. Single K+ channels from Streptomyces lividans: functional asymmetries and sidedness of proton activation. J. Gen. Physiol. 114, 551–560 (1999). · DOI
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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
Self-citationStockbridge, R. B., & Wackett, L. P. (2024) · Nature Communications · doi:10.1038/s41467-024-49018-1 · Cited by 80
Self-citationMembrane 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
Self-citationHu, M., & Scott, C. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.00157-24 · Cited by 63
Metadata
- Authors
- Stockbridge, R. B., Koide, A., Miller, C., & Koide, S.
- Venue
- Nature Communications
- Published
- 2014-10-07
- Volume
- 5
- Issue
- 1
- ISSN
- 2041-1723
- PMC
- PMC4265568
- Cited by
- 55
- References
- 1
- Language
- en
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