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 Van Rossum, Kutti R. Vinothkumar, Lieselotte Handel, Gregorio Giuseppe De Palma, Benjamin Bardiaux, Guido Pintacuda, Lyndon Emsley, Werner Kühlbrandt, Hartmut Oschkinat

Research output: Contribution to journalArticlepeer-review

53 Scopus citations


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.

Original languageEnglish (US)
Article number2073
JournalNature communications
Issue number1
StatePublished - Dec 1 2017
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)


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