Ontology highlight
ABSTRACT:
SUBMITTER: Retel JS
PROVIDER: S-EPMC5727033 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Retel Joren S JS Nieuwkoop Andrew J AJ Hiller Matthias M Higman Victoria A VA Barbet-Massin Emeline E Stanek Jan J Andreas Loren B LB Franks W Trent WT van Rossum Barth-Jan BJ Vinothkumar Kutti R KR Handel Lieselotte L de Palma Gregorio Giuseppe GG Bardiaux Benjamin B Pintacuda Guido G Emsley Lyndon L Kühlbrandt Werner W Oschkinat Hartmut H
Nature communications 20171212 1
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-res ...[more]