Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/44522
Title: Structure of outer membrane protein G in lipid bilayers.
Authors: Retel, JS
Nieuwkoop, AJ
Hiller, M
Higman, VA
Barbet-Massin, E
Stanek, J
Andreas, LB
Franks, WT
van Rossum, B-J
Vinothkumar, KR
Handel, L
de Palma, GG
Bardiaux, B
Pintacuda, G
Emsley, L
Kühlbrandt, W
Oschkinat, H
First Published: 12-Dec-2017
Publisher: Nature Research (part of Springer Nature)
Citation: Nature Communications, 2017, 8, Article number: 2073
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.
DOI Link: 10.1038/s41467-017-02228-2
eISSN: 2041-1723
Links: https://www.nature.com/articles/s41467-017-02228-2
http://hdl.handle.net/2381/44522
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2017. This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Description: All relevant data necessary for producing the samples, assigning the protein signals, and calculating the structures are available from the corresponding author upon reasonable request. The NMR data and protein structure are deposited in the BioMagResBank (BMRB) with ID 34088 and the Protein Data Bank (PDB) with ID 5MWV, respectively. The script is deposited in GitHub and can be downloaded under: https://github.com/jorenretel/ompg_restraint_generation.
Appears in Collections:Published Articles, Dept. of Molecular and Cell Biology

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