Structure of outer membrane protein G in lipid bilayers.

Retel, J. S.; Nieuwkoop, A. J.; Hiller, M.; Higman, V. A.; Barbet-Massin, E.; Stanek, J.; Andreas, L. B.; Franks, W. T.; van Rossum, B. J.; Vinothkumar, K. R.; Handel, L.; de Palma, G. G.; Bardiaux, B.; Pintacuda, G.; Emsley, L.; Kühlbrandt, W.; Oschkinat, H.

doi:10.1038/s41467-017-02228-2

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Structure of outer membrane protein G in lipid bilayers.

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Andreas, L. B.
Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Retel, J. S., Nieuwkoop, A. J., Hiller, M., Higman, V. A., Barbet-Massin, E., Stanek, J., et al. (2017). Structure of outer membrane protein G in lipid bilayers. Nature Communications, 8: 2073. doi:10.1038/s41467-017-02228-2.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002E-9051-3

Abstract

β-barrel proteins mediate nutrient uptake in bacteria and serve vital functions in cell signaling and adhesion. For the 14-strand outer membrane protein G of Escherichia coli, opening and closing is pH-dependent. Different roles of the extracellular loops in this process were proposed, and X-ray and solution NMR studies were divergent. Here, we report the structure of outer membrane protein G investigated in bilayers of E. coli lipid extracts by magic-angle-spinning NMR. In total, 1847 inter-residue 1H–1H and 13C–13C distance restraints, 256 torsion angles, but no hydrogen bond restraints are used to calculate the structure. The length of β-strands is found to vary beyond the membrane boundary, with strands 6–8 being the longest and the extracellular loops 3 and 4 well ordered. The site of barrel closure at strands 1 and 14 is more disordered than most remaining strands, with the flexibility decreasing toward loops 3 and 4. Loop 4 presents a well-defined helix.