Publication

Article Metrics

Citations


Online attention

Combined 1 H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments

DOI: 10.1016/j.str.2017.11.011 DOI Help

Authors: Lindsay A. Baker (Utrecht University; University of Oxford) , Tessa Sinnige (Utrecht University) , Pascale Schellenberger (University of Oxford) , Jeanine De Keyzer (Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen; The Zernike Institute for Advanced Materials) , C. Alistair Siebert (University of Oxford) , Arnold J. M. Driessen (Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen; The Zernike Institute for Advanced Materials) , Marc Baldus (Utrecht University) , Kay Grunewald (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure , VOL 26 , PAGES 161 - 170.e3

State: Published (Approved)
Published: January 2018
Diamond Proposal Number(s): 14856

Open Access Open Access

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.

Journal Keywords: membrane proteins; solid-state NMR; electron cryotomography; YidC; hybrid methods; native membranes; MAS

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: M01-Polara at OPIC (Oxford) , Krios I-Titan Krios I at Diamond

Documents:
1-s2.0-S0969212617303647-main.pdf