- Structure of outer membrane protein G in lipid bilayers.
Structure of outer membrane protein G in lipid bilayers.
Nature communications (2017-12-14)
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
PMID29233991
ZUSAMMENFASSUNG
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
MATERIALIEN