期刊
NATURE
卷 525, 期 7570, 页码 548-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature14981
关键词
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资金
- Wellcome Trust [102890/Z/13/Z]
- National Institutes of Health (NIH) [RO1-GM107023, U54-GM087519]
- NIH [K99-GM-111767]
To contend with hazards posed by environmental fluoride, microorganisms export this anion through F--specific ion channels of the Fluc family(1-4). 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(5,6). 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 angstrom. 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+center dot 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.
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