期刊
SCIENCE ADVANCES
卷 9, 期 34, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.adg9709
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In this study, ssNMR and molecular dynamics simulations were used to investigate the fluoride channel Fluc-Ec1 in phospholipid bilayers. Previously unidentified fluoride binding sites and a water molecule binding site in the polar track were discovered. Additionally, a dynamic hotspot at loop 1 was observed, suggesting that loop 1 is a key determinant for channel gating.
Solid-state nuclear magnetic resonance (ssNMR) methods can probe the motions of membrane proteins in liposomes at the atomic level and propel the understanding of biomolecular processes for which static structures cannot provide a satisfactory description. In this work, we report our study on the fluoride channel Fluc-Ec1 in phospholipid bilayers based on ssNMR and molecular dynamics simulations. Previously unidentified fluoride binding sites in the aqueous vestibules were experimentally verified by 19F-detected ssNMR. One of the two fluoride binding sites in the polar track was identified as a water molecule by 1H-detected ssNMR. Meanwhile, a dynamic hotspot at loop 1 was observed by comparing the spectra of wild-type Fluc-Ec1 in variant buffer conditions or with its mutants. Therefore, we propose that fluoride conduction in the Fluc channel occurs via a water-mediated knock-on permeation mechanism and that loop 1 is a key molecular determinant for channel gating.
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