Joren Sebastian 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 Ragunath Vinothkumar, Lieselotte Handel, Gregorio Giuseppe de Palma, Benjamin Bardiaux, Guido Pintacuda, Lyndon Emsley, Werner Kühlbrandt, Hartmut Oschkinat
- 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.
MetadatenVerfasserangaben: | Joren Sebastian 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 Ragunath VinothkumarORCiDGND, Lieselotte Handel, Gregorio Giuseppe de Palma, Benjamin BardiauxORCiD, Guido Pintacuda, Lyndon Emsley, Werner KühlbrandtORCiDGND, Hartmut Oschkinat |
---|
URN: | urn:nbn:de:hebis:30:3-456091 |
---|
DOI: | https://doi.org/10.1038/s41467-017-02228-2 |
---|
ISSN: | 2041-1723 |
---|
Pubmed-Id: | https://pubmed.ncbi.nlm.nih.gov/29233991 |
---|
Titel des übergeordneten Werkes (Englisch): | Nature Communications |
---|
Verlag: | Nature Publishing Group UK |
---|
Verlagsort: | [London] |
---|
Dokumentart: | Wissenschaftlicher Artikel |
---|
Sprache: | Englisch |
---|
Jahr der Fertigstellung: | 2017 |
---|
Datum der Erstveröffentlichung: | 12.12.2017 |
---|
Veröffentlichende Institution: | Universitätsbibliothek Johann Christian Senckenberg |
---|
Datum der Freischaltung: | 01.02.2018 |
---|
Freies Schlagwort / Tag: | Protein folding; Solid-state NMR |
---|
Jahrgang: | 8 |
---|
Ausgabe / Heft: | 1, Art. 2073 |
---|
Seitenzahl: | 10 |
---|
Erste Seite: | 1 |
---|
Letzte Seite: | 10 |
---|
Bemerkung: | 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 |
---|
HeBIS-PPN: | 426623819 |
---|
Institute: | Biochemie, Chemie und Pharmazie / Biochemie und Chemie |
---|
| Angeschlossene und kooperierende Institutionen / MPI für Biophysik |
---|
DDC-Klassifikation: | 5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften |
---|
Sammlungen: | Universitätspublikationen |
---|
Lizenz (Deutsch): | Creative Commons - Namensnennung 4.0 |
---|