5A40
Crystal structure of a dual topology fluoride ion channel.
Summary for 5A40
| Entry DOI | 10.2210/pdb5a40/pdb |
| Related | 5A41 5A43 |
| Descriptor | PUTATIVE FLUORIDE ION TRANSPORTER CRCB, MONOBODIES, MERCURY (II) ION (3 entities in total) |
| Functional Keywords | transport protein, fluoride ion channel, monobody, bpe |
| Biological source | BORDETELLA PERTUSSIS More |
| Cellular location | Cell inner membrane ; Multi-pass membrane protein : Q7VYU0 |
| Total number of polymer chains | 8 |
| Total formula weight | 94109.70 |
| 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: 2024-05-08) |
| Primary citation | Stockbridge, 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: 26344196DOI: 10.1038/NATURE14981 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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