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5A43

Crystal structure of a dual topology fluoride ion channel.

Summary for 5A43
Entry DOI10.2210/pdb5a43/pdb
Related5A40 5A41
DescriptorPUTATIVE FLUORIDE ION TRANSPORTER CRCB, MONOBODIES, FLUORIDE ION, ... (6 entities in total)
Functional Keywordstransport protein, fluoride ion channel, fluc, ec2
Biological sourceESCHERICHIA COLI S88
More
Cellular locationCell inner membrane ; Multi-pass membrane protein : B7LI20
Total number of polymer chains4
Total formula weight49965.43
Authors
Stockbridge, R.B.,Kolmakova-Partensky, L.,Shane, T.,Koide, A.,Koide, S.,Miller, C.,Newstead, S. (deposition date: 2015-06-04, release date: 2015-09-02, Last modification date: 2024-11-13)
Primary citationStockbridge, R.B.,Kolmakova-Partensky, L.,Shane, T.,Koide, A.,Koide, S.,Miller, C.,Newstead, S.
Crystal Structures of a Double-Barrelled Fluoride Ion Channel.
Nature, 525:548-, 2015
Cited by
PubMed Abstract: To contend with hazards posed by environmental fluoride, microorganisms export this anion through F(-)-specific ion channels of the Fluc family. Since the recent discovery of Fluc channels, numerous idiosyncratic features of these proteins have been unearthed, including strong selectivity for F(-) over Cl(-) and dual-topology dimeric assembly. To understand the chemical basis for F(-) permeation and how the antiparallel subunits convene to form a F(-)-selective pore, here we solve the crystal structures of two bacterial Fluc homologues in complex with three different monobody inhibitors, with and without F(-) present, to a maximum resolution of 2.1 Å. The structures reveal a surprising 'double-barrelled' channel architecture in which two F(-) ion pathways span the membrane, and the dual-topology arrangement includes a centrally coordinated cation, most likely Na(+). F(-) selectivity is proposed to arise from the very narrow pores and an unusual anion coordination that exploits the quadrupolar edges of conserved phenylalanine rings.
PubMed: 26344196
DOI: 10.1038/NATURE14981
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.58 Å)
Structure validation

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