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A topologically diverse family of fluoride channels
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The fluoride channel family encompasses a topologically diverse set of proteins that provide an unusual glimpse into evolutionary processes in membrane transport proteins.
“The fluoride channel family encompasses a topologically diverse set of proteins that provide an unusual glimpse into evolutionary processes in membrane transport proteins(68) (Figure 5a).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [68]
Among bacterial Flucs, gene duplications have occurred on at least five occasions.
“In addition to the dual topology homodimers, among bacterial Flucs, gene duplications have occurred on at least five occasions (68);”
From Membrane exporters of fluoride ion (2021) · cites this paper as [68]
Fluc proteins can be encoded by single genes forming antiparallel homodimers, or by paired genes forming heterodimers of obligate inward- and outward-facing subunits.
“Fluc proteins can be encoded by single genes, in which case a single protomer is inserted into the membrane in both inward and outward-facing conformations, assembling as an antiparallel homodimer, or they can be encoded by paired genes that express to form heterodimers of obligate inward- and outward-facing subunits84.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [84]
Typically, genes for heterodimeric Flucs are adjacent in genomes, and both genes are required for fluoride efflux activity.
“Typically, the genes for the heterodimeric Flucs are adjacent to each other in genomes, and both genes are required for fluoride efflux activity84.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [84]
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Citations
Cites
Metal–ligand geometry relevant to proteins and in proteins: sodium and potassium
Harding, M. M. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902003712 · Cited by 279
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-citationBacterial fluoride resistance, Fluc channels, and the weak acid accumulation effect
Ji, C., Stockbridge, R. B., & Miller, C. (2014) · Journal of General Physiology · doi:10.1085/jgp.201411243 · Cited by 97
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Cited by
Sorted by citations
Stockbridge, 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-citationBanerjee, A., Kang, C.-Y., An, M., Koff, B. B., Sunder, S., Kumar, A., Tenuta, L. M. A., & Stockbridge, R. B. (2024) · mBio · doi:10.1128/mbio.00184-24 · Cited by 17
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Metadata
- Authors
- Macdonald, C. B., & Stockbridge, R. B.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2017-08
- Volume
- 45
- Pages
- 142-149
- ISSN
- 0959-440X
- PMC
- PMC5612848
- Cited by
- 21
- References
- 3
- Language
- en
- Funders
- National Institutes of Health (R00GM111767)
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