TY  - JOUR
AU  - Zhang, Jin
AU  - Song, Dan
AU  - Schackert, Florian Karl
AU  - Li, Juan
AU  - Xiang, Shengqi
AU  - Tian, Changlin
AU  - Gong, Weimin
AU  - Carloni, Paolo
AU  - Alfonso-Prieto, Mercedes
AU  - Shi, Chaowei
TI  - Fluoride permeation mechanism of the Fluc channel in liposomes revealed by solid-state NMR
JO  - Science advances
VL  - 9
IS  - 34
SN  - 2375-2548
CY  - Washington, DC [u.a.]
PB  - Assoc.
M1  - FZJ-2023-03186
SP  - eadg9709
PY  - 2023
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 37611110
UR  - <Go to ISI:>//WOS:001053144500018
DO  - DOI:10.1126/sciadv.adg9709
UR  - https://juser.fz-juelich.de/record/1010678
ER  -