TY  - JOUR
A1  - Retel, Joren Sebastian
A1  - Nieuwkoop, Andrew J.
A1  - Hiller, Matthias
A1  - Higman, Victoria A.
A1  - Barbet-Massin, Emeline
A1  - Stanek, Jan
A1  - Andreas, Loren B.
A1  - Franks, W. Trent
A1  - Rossum, Barth-Jan van
A1  - Vinothkumar, Kutti Ragunath
A1  - Handel, Lieselotte
A1  - Palma, Gregorio Giuseppe de
A1  - Bardiaux, Benjamin
A1  - Pintacuda, Guido
A1  - Emsley, Lyndon
A1  - Kühlbrandt, Werner
A1  - Oschkinat, Hartmut
T1  - Structure of outer membrane protein G in lipid bilayers
T2  - Nature Communications
N2  - 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.
KW  - Protein folding
KW  - Solid-state NMR
Y1  - 2017
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/45609
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-456091
SN  - 2041-1723
N1  - Open Access: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/. © The Author(s) 2017
VL  - 8
IS  - 1, Art. 2073
SP  - 1
EP  - 10
PB  - Nature Publishing Group UK
CY  - [London]
ER  -