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  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., et al. (2017). Structure of outer membrane protein G in lipid bilayers. Nature Communications, 8: 2073. doi:10.1038/s41467-017-02228-2.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-9051-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-487C-4
Genre: Journal Article

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 Creators:
Retel, J. S., Author
Nieuwkoop, A. J., Author
Hiller, M., Author
Higman, V. A., Author
Barbet-Massin, E., Author
Stanek, J., Author
Andreas, L. B.1, Author              
Franks, W. T., Author
van Rossum, B. J., Author
Vinothkumar, K. R., Author
Handel, L., Author
de Palma, G. G., Author
Bardiaux, B., Author
Pintacuda, G., Author
Emsley, L., Author
Kühlbrandt, W., Author
Oschkinat, H., Author
Affiliations:
1Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              

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 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.

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Language(s): eng - English
 Dates: 2017-12-12
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-017-02228-2
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Title: Nature Communications
Source Genre: Journal
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Pages: 10 Volume / Issue: 8 Sequence Number: 2073 Start / End Page: - Identifier: -