Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy Export

@article{citeulike:2609559, abstract = {Intermolecular nuclear Overhauser effects (NOEs) between the integral outer membrane protein OmpX from Escherichia coli and dihexanoylphosphatidylcholine (DHPC) provided a detailed description of protein-detergent interactions. The NOEs were measured in 3D 15N- and 13C-resolved [1H,1H]-NOESY spectra recorded with selectively methyl-protonated and otherwise uniformly 2H,13C,15N-labeled OmpX in micelles of DHPC at natural isotope abundance. In these mixed micelles the NMR structure of OmpX consists of an eight-stranded antiparallel [beta]-barrel. The OmpX surface area covered with intermolecular NOEs to the DHPC hydrophobic tails forms a continuous cylinder jacket of approximately 28 A in height, which is centered about the middle of the long axis through the [beta]-barrel. In addition, some intermolecular NOEs with methyl groups of the DHPC polar head were identified along both boundaries of this cylinder jacket. The experimental data suggest that the hydrophobic surface areas of OmpX are covered with a monolayer of DHPC molecules, which appears to mimic quite faithfully the embedding of the [beta]-barrel in a double-layer lipid membrane. 10.1073/pnas.212515099}, author = {Fernandez, Cesar and Hilty, Christian and Wider, Gerhard and Wuthrich, Kurt}, citeulike-article-id = {2609559}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.212515099}, citeulike-linkout-1 = {http://www.pnas.org/content/99/21/13533.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/99/21/13533.full.pdf}, citeulike-linkout-3 = {http://www.pnas.org/cgi/content/abstract/99/21/13533}, citeulike-linkout-4 = {http://view.ncbi.nlm.nih.gov/pubmed/12370417}, citeulike-linkout-5 = {http://www.hubmed.org/display.cgi?uids=12370417}, day = {15}, doi = {10.1073/pnas.212515099}, journal = {Proceedings of the National Academy of Sciences}, keywords = {dhpc, interactions, lipid, membrane, nmr, protein}, month = {October}, number = {21}, pages = {13533--13537}, posted-at = {2008-09-01 05:25:45}, priority = {2}, title = {Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy}, url = {http://dx.doi.org/10.1073/pnas.212515099}, volume = {99}, year = {2002} }

TY - JOUR ID - citeulike:2609559 L3 - citeulike-article-id:2609559 N2 - Intermolecular nuclear Overhauser effects (NOEs) between the integral outer membrane protein OmpX from Escherichia coli and dihexanoylphosphatidylcholine (DHPC) provided a detailed description of protein-detergent interactions. The NOEs were measured in 3D 15N- and 13C-resolved [1H,1H]-NOESY spectra recorded with selectively methyl-protonated and otherwise uniformly 2H,13C,15N-labeled OmpX in micelles of DHPC at natural isotope abundance. In these mixed micelles the NMR structure of OmpX consists of an eight-stranded antiparallel [beta]-barrel. The OmpX surface area covered with intermolecular NOEs to the DHPC hydrophobic tails forms a continuous cylinder jacket of approximately 28 A in height, which is centered about the middle of the long axis through the [beta]-barrel. In addition, some intermolecular NOEs with methyl groups of the DHPC polar head were identified along both boundaries of this cylinder jacket. The experimental data suggest that the hydrophobic surface areas of OmpX are covered with a monolayer of DHPC molecules, which appears to mimic quite faithfully the embedding of the [beta]-barrel in a double-layer lipid membrane. 10.1073/pnas.212515099 IS - 21 JF - Proceedings of the National Academy of Sciences EP - 13537 TI - Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy VL - 99 SP - 13533 KW - dhpc KW - interactions KW - lipid KW - membrane KW - nmr KW - protein AU - Fernandez, Cesar AU - Hilty, Christian AU - Wider, Gerhard AU - Wuthrich, Kurt PY - 2002/10/15/ UR - http://dx.doi.org/10.1073/pnas.212515099 ER -