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Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation

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Abstract

Solid-state NMR studies of sedimented soluble proteins has been developed recently as an attractive approach for overcoming the size limitations of solution NMR spectroscopy while bypassing the need for sample crystallization or precipitation (Bertini et al. Proc Natl Acad Sci USA 108(26):10396–10399, 2011). Inspired by the potential benefits of this method, we have investigated the ability to sediment lipid bilayer nanodiscs reconstituted with a membrane protein. In this study, we show that nanodiscs containing the outer membrane protein Ail from Yersinia pestis can be sedimented for solid-state NMR structural studies, without the need for precipitation or lyophilization. Optimized preparations of Ail in phospholipid nanodiscs support both the structure and the fibronectin binding activity of the protein. The same sample can be used for solution NMR, solid-state NMR and activity assays, facilitating structure–activity correlation experiments across a wide range of timescales.

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Acknowledgments

We thank Bibhuti Das, Chris Grant, Chin Wu and Stan Opella for assistance with solid-state NMR experiments. This research was supported by Grants from the National Institutes of Health (GM100265; P41 EB002031; P30 CA030199).

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  1. Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037, USA

    Yi Ding, L. Miya Fujimoto, Yong Yao & Francesca M. Marassi

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Correspondence to Francesca M. Marassi.

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Ding, Y., Fujimoto, L.M., Yao, Y. et al. Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation. J Biomol NMR 61, 275–286 (2015). https://doi.org/10.1007/s10858-014-9893-4

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