Combined 1H-Detected Solid-State NMR.pdf (6.17 MB)
Combined 1H-Detected solid-state NMR spectroscopy and electron cryotomography to study membrane proteins across resolutions in native environments
journal contribution
posted on 2023-06-09, 09:07 authored by Lindsay A Baker, Tessa Sinnige, Pascale Schellenberger, Jeanine de Keyzer, C Alistair Siebert, Arnold J M Driessen, Marc Baldus, Kay GrünewaldMembrane proteins remain challenging targets for structural biology, despite much effort, as their native environment is heterogeneous and complex. Most methods rely on detergents to extract membrane proteins from their native environment, but this removal can significantly alter the structure and function of these proteins. Here, we overcome these challenges with a hybrid method to study membrane proteins in their native membranes, combining high-resolution solid-state nuclear magnetic resonance spectroscopy and electron cryotomography using the same sample. Our method allows the structure and function of membrane proteins to be studied in their native environments, across different spatial and temporal resolutions, and the combination is more powerful than each technique individually. We use the method to demonstrate that the bacterial membrane protein YidC adopts a different conformation in native membranes and that substrate binding to YidC in these native membranes differs from purified and reconstituted systems
History
Publication status
- Published
File Version
- Published version
Journal
StructureISSN
0969-2126Publisher
ElsevierExternal DOI
Issue
1Volume
26Page range
161-170Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2018-03-08First Open Access (FOA) Date
2018-03-13First Compliant Deposit (FCD) Date
2018-03-12Usage metrics
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