Structure of outer membrane protein G in lipid bilayers.

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 extracell

SUBMITTER: Retel JS 

PROVIDER: S-EPMC5727033 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature