Combined 1H-Detected solid-state NMR spectroscopy and electron cryotomography to study membrane proteins across resolutions in native environments

Baker, Lindsay A, Sinnige, Tessa, Schellenberger, Pascale, de Keyzer, Jeanine, Siebert, C Alistair, Driessen, Arnold J M, Baldus, Marc and Grünewald, Kay (2018) Combined 1H-Detected solid-state NMR spectroscopy and electron cryotomography to study membrane proteins across resolutions in native environments. Structure, 26 (1). pp. 161-170. ISSN 0969-2126

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Abstract

Membrane 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

Item Type: Article
Keywords: MAS; YidC; electron cryotomography; hybrid methods; membrane proteins; native membranes; solid-state NMR
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science > Q Science (General)
Related URLs:
Depositing User: Pascale Schellenberger
Date Deposited: 08 Mar 2018 10:58
Last Modified: 13 Mar 2018 14:56
URI: http://sro.sussex.ac.uk/id/eprint/71682

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