Use of paramagnetic 19F NMR to monitor domain movement in a glutamate transporter homolog

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 w...

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Published inNature chemical biology Vol. 16; no. 9; pp. 1006 - 1012
Main Authors Huang, Yun, Wang, Xiaoyu, Lv, Guohua, Razavi, Asghar M., Huysmans, Gerard H. M., Weinstein, Harel, Bracken, Clay, Eliezer, David, Boudker, Olga
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.09.2020
Nature Publishing Group
Subjects
631/535/878
631/57
631/92/577
Accessibility
Binding sites
Biochemical Engineering
Biochemistry
Bioorganic Chemistry
Cell Biology
Chelation
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Glutamic acid transporter
Histidine
Homology
Magnetic resonance spectroscopy
Membrane proteins
NMR
NMR spectroscopy
Nuclear magnetic resonance
Nuclei
Protein transport
Proteins
Substrates
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Abstract 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.
AbstractList 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 19F-NMR spectroscopy approach to probe dynamics of large membrane proteins. We labeled a glutamate transporter homolog with a 19F probe via cysteine chemistry and with a Ni2+ ion via chelation by a di-histidine motif. We used distance-dependent enhancement of the longitudinal relaxation of 19F 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 19F nuclei.
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.
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 19F-NMR spectroscopy approach to probe dynamics of large membrane proteins. We labeled a glutamate transporter homolog with a 19F probe via cysteine chemistry and with a Ni2+ ion via chelation by a di-histidine motif. We used distance-dependent enhancement of the longitudinal relaxation of 19F 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 19F nuclei.A 19F-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.
Author Lv, Guohua
Weinstein, Harel
Razavi, Asghar M.
Eliezer, David
Wang, Xiaoyu
Huang, Yun
Huysmans, Gerard H. M.
Boudker, Olga
Bracken, Clay
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Snippet In proteins where conformational changes are functionally important, the number of accessible states and their dynamics are often difficult to establish. Here...
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SubjectTerms 631/535/878
631/57
631/92/577
Accessibility
Binding sites
Biochemical Engineering
Biochemistry
Bioorganic Chemistry
Cell Biology
Chelation
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Glutamic acid transporter
Histidine
Homology
Magnetic resonance spectroscopy
Membrane proteins
NMR
NMR spectroscopy
Nuclear magnetic resonance
Nuclei
Protein transport
Proteins
Substrates
Title Use of paramagnetic 19F NMR to monitor domain movement in a glutamate transporter homolog
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