Unknown

Dataset Information

0

Structure of outer membrane protein G in lipid bilayers.


ABSTRACT: ?-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 ?-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.

SUBMITTER: Retel JS 

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

REPOSITORIES: biostudies-literature

altmetric image

Publications


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]

Similar Datasets

| S-EPMC5713880 | biostudies-literature
| S-EPMC4281492 | biostudies-literature
| S-EPMC7232533 | biostudies-literature
| S-EPMC3233656 | biostudies-literature
| S-EPMC6042154 | biostudies-literature
| S-EPMC4571027 | biostudies-literature
| S-EPMC5371976 | biostudies-literature
| S-EPMC8580007 | biostudies-literature
| S-EPMC6819253 | biostudies-literature
| S-EPMC3202590 | biostudies-literature