Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR
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Publication date
2015-06-30
Authors
Kaplan, M.
Cukkemane, Abhishek
Van Zundert, Gydo C P
Narasimhan, Siddarth
Daniels, Mark
Mance, Deni
Waksman, Gabriel
Bonvin, Alexandre M J J
Fronzes, Rémi
Folkers, Gert
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Article
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Abstract
Studying biomolecules at atomic resolution in their native environment is the ultimate aim of structural biology. We investigated the bacterial type IV secretion system core complex (T4SScc) by cellular dynamic nuclear polarization-based solid-state nuclear magnetic resonance spectroscopy to validate a structural model previously generated by combining in vitro and in silico data. Our results indicate that T4SScc is well folded in the cellular setting, revealing protein regions that had been elusive when studied in vitro.
Keywords
Taverne, Biotechnology, Molecular Biology, Biochemistry, Cell Biology, General Medicine
Citation
Kaplan, M, Cukkemane, A, Van Zundert, G C P, Narasimhan, S, Daniëls, M, Mance, D, Waksman, G, Bonvin, A M J J, Fronzes, R, Folkers, G E & Baldus, M 2015, 'Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR', Nature Methods, vol. 12, no. 7, pp. 649-652. https://doi.org/10.1038/nmeth.3406