ArticleBiochimica et biophysica acta2007
NMR structural studies of the bacterial outer membrane protein OmpX in oriented lipid bilayer membranes.
Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Recombinant Expression and Overproduction of Transmembrane β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Photoradical-Mediated Catalyst-Independent Protein Cross-Link with Unusual Fluorescence Properties.Chembiochem : a European journal of chemical biology · 2023Article
- Article
- Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017Review
- High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes.Journal of biomolecular NMR · 2017Article
- Membrane protein structure determination in membrana.Accounts of chemical research · 2013Article
- Charge asymmetry in the proteins of the outer membrane.Bioinformatics (Oxford, England) · 2013Article
- Membrane protein structure determination: back to the membrane.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel.Scientific reports · 2013Article
- Methionine mutations of outer membrane protein X influence structural stability and beta-barrel unfolding.PloS one · 2013Article
- Structure determination of a membrane protein in proteoliposomes.Journal of the American Chemical Society · 2012Article
- Physical determinants of β-barrel membrane protein folding in lipid vesicles.Biophysical journal · 2011Article
- Expression, refolding, and initial structural characterization of the Y. pestis Ail outer membrane protein in lipids.Biochimica et biophysica acta · 2011Article
- Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.Molecular bioSystems · 2009Review
- Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro.The Journal of biological chemistry · 2008Article
- Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.Biochemistry · 2008Article
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Authors and funding
4 authors.
Funding
Abstract
The beta-barrels found in the outer membranes of prokaryotic and eukaryotic organisms constitute an important functional class of proteins. Here we present solid-state NMR spectra of the bacterial outer membrane protein OmpX in oriented lipid bilayer membranes. We show that OmpX is folded in both glass-supported oriented lipid bilayers and in lipid bicelles that can be magnetically oriented with the membrane plane parallel or perpendicular to the direction of the magnetic field. The presence of resolved peaks in these spectra demonstrates that OmpX undergoes rotational diffusion around an axis perpendicular to the membrane surface. A tightly hydrogen-bonded domain of OmpX resists exchange with D2O for days and is assigned to the transmembrane beta-barrel, while peaks at isotropic resonance frequencies that disappear rapidly in D2O are assigned to the extracellular and periplasmic loops. The two-dimensional 1H/15N separated local field spectra of OmpX have several resolved peaks, and agree well with the spectra calculated from the crystal structure of OmpX rotated with the barrel axis nearly parallel (5 degrees tilt) to the direction of the magnetic field. The data indicate that it will be possible to obtain site-specific resonance assignments and to determine the structure, tilt, and rotation of OmpX in membranes using the solid-state NMR methods that are currently being applied to alpha-helical membrane proteins.
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