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Article Dans Une Revue Nature Communications Année : 2017

Structure of outer membrane protein G in lipid bilayers

Résumé

beta-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 H-1-H-1 and C-13-C-13 distance restraints, 256 torsion angles, but no hydrogen bond restraints are used to calculate the structure. The length of beta-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.
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hal-01679641 , version 1 (03-10-2018)

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Joren Retel, Andrew J. Nieuwkoop, Matthias Hiller, Victoria A. Higman, Emeline Barbet-Massin, et al.. Structure of outer membrane protein G in lipid bilayers. Nature Communications, 2017, 8 (1), pp.Article Number: 2073. ⟨10.1038/s41467-017-02228-2⟩. ⟨hal-01679641⟩
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