Structure of outer membrane protein G in lipid bilayers

Joren S. Retel, Andrew J. Nieuwkoop, Matthias Hiller, Victoria A. Higman, Emeline Barbet-Massin, Jan Stanek, Loren B. Andreas, W. Trent Franks, Barth-Jan Rossum, Kutti R. Vinothkumar, Lieselotte Handel, Gregorio Giuseppe Palma, Benjamin Bardiaux, Guido Pintacuda, Lyndon Emsley, Werner Kühlbrandt and Hartmut Oschkinat ()
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Joren S. Retel: Leibniz-Institut für Molekulare Pharmakologie
Andrew J. Nieuwkoop: Leibniz-Institut für Molekulare Pharmakologie
Matthias Hiller: Leibniz-Institut für Molekulare Pharmakologie
Victoria A. Higman: Leibniz-Institut für Molekulare Pharmakologie
Emeline Barbet-Massin: Université de Lyon
Jan Stanek: Université de Lyon
Loren B. Andreas: Université de Lyon
W. Trent Franks: Leibniz-Institut für Molekulare Pharmakologie
Barth-Jan Rossum: Leibniz-Institut für Molekulare Pharmakologie
Kutti R. Vinothkumar: Max-Planck-Institut für Biophysik
Lieselotte Handel: Leibniz-Institut für Molekulare Pharmakologie
Gregorio Giuseppe Palma: Leibniz-Institut für Molekulare Pharmakologie
Benjamin Bardiaux: Leibniz-Institut für Molekulare Pharmakologie
Guido Pintacuda: Université de Lyon
Lyndon Emsley: Université de Lyon
Werner Kühlbrandt: Max-Planck-Institut für Biophysik
Hartmut Oschkinat: Leibniz-Institut für Molekulare Pharmakologie

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: 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.

Date: 2017
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DOI: 10.1038/s41467-017-02228-2

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