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Use of paramagnetic 19F NMR to monitor domain movement in a glutamate transporter homolog
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Use of paramagnetic 19F NMR to monitor domain movement in a glutamate transporter homolog
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Use of paramagnetic 19F NMR to monitor domain movement in a glutamate transporter homolog
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Journal Article
Use of paramagnetic 19F NMR to monitor domain movement in a glutamate transporter homolog
2020
Overview
In proteins where conformational changes are functionally important, the number of accessible states and their dynamics are often difficult to establish. Here we describe a novel
19
F-NMR spectroscopy approach to probe dynamics of large membrane proteins. We labeled a glutamate transporter homolog with a
19
F probe via cysteine chemistry and with a Ni
2+
ion via chelation by a di-histidine motif. We used distance-dependent enhancement of the longitudinal relaxation of
19
F nuclei by the paramagnetic metal to assign the observed resonances. We identified one inward- and two outward-facing states of the transporter, in which the substrate-binding site is near the extracellular and intracellular solutions, respectively. We then resolved the structure of the unanticipated second outward-facing state by cryo-EM. Finally, we showed that the rates of the conformational exchange are accessible from measurements of the metal-enhanced longitudinal relaxation of
19
F nuclei.
A
19
F-NMR-based method monitoring the conformational dynamics of the glutamate transporter GltPh identified one inward- and two outward-facing states, including one unanticipated outward-facing state that was characterized by cryo-EM.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
