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001010678 1001_ $$0P:(DE-HGF)0$$aZhang, Jin$$b0
001010678 245__ $$aFluoride permeation mechanism of the Fluc channel in liposomes revealed by solid-state NMR
001010678 260__ $$aWashington, DC [u.a.]$$bAssoc.$$c2023
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001010678 520__ $$aSolid-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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001010678 7001_ $$00000-0003-3686-9042$$aSong, Dan$$b1
001010678 7001_ $$0P:(DE-Juel1)180424$$aSchackert, Florian Karl$$b2
001010678 7001_ $$0P:(DE-HGF)0$$aLi, Juan$$b3
001010678 7001_ $$00000-0002-6874-4925$$aXiang, Shengqi$$b4
001010678 7001_ $$0P:(DE-HGF)0$$aTian, Changlin$$b5
001010678 7001_ $$00000-0002-6723-1298$$aGong, Weimin$$b6
001010678 7001_ $$0P:(DE-Juel1)145614$$aCarloni, Paolo$$b7
001010678 7001_ $$0P:(DE-Juel1)169976$$aAlfonso-Prieto, Mercedes$$b8
001010678 7001_ $$00000-0002-0024-1096$$aShi, Chaowei$$b9$$eCorresponding author
001010678 773__ $$0PERI:(DE-600)2810933-8$$a10.1126/sciadv.adg9709$$gVol. 9, no. 34, p. eadg9709$$n34$$peadg9709$$tScience advances$$v9$$x2375-2548$$y2023
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