@article{Kleinschmidt2008Prote-8118,
  year={2008},
  doi={10.1021/bi800750s},
  title={Protein-Lipid Interactions with Fusobacterium nucleatum Major Outer Membrane Protein FomA : Spin-Label EPR and Polarized Infrared Spectroscopy},
  number={37},
  volume={47},
  issn={0006-2960},
  journal={Biochemistry},
  pages={8414--8423},
  author={Kleinschmidt, Jörg and Marsh, Derek and Vijay, N. and Anbazhagan, Veerappan}
}

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    <dc:creator>Vijay, N.</dc:creator>
    <dc:creator>Marsh, Derek</dc:creator>
    <dcterms:bibliographicCitation>First publ. in: Biochemistry ; 47 (2008), 37. - S. 8414 8423</dcterms:bibliographicCitation>
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    <dc:contributor>Anbazhagan, Veerappan</dc:contributor>
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    <dcterms:issued>2008</dcterms:issued>
    <dcterms:title>Protein-Lipid Interactions with Fusobacterium nucleatum Major Outer Membrane Protein FomA : Spin-Label EPR and Polarized Infrared Spectroscopy</dcterms:title>
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    <dc:creator>Anbazhagan, Veerappan</dc:creator>
    <dcterms:abstract xml:lang="eng">FomA, the major outer membrane protein of Fusobacterium nucleatum, was expressed and purified in Escherichia coli and reconstituted from detergent in bilayer membranes of phosphatidylcholines with chain lengths from C(12:0) to C(17:0). The conformation and orientation of membrane-incorporated FomA were determined from polarized, attenuated total reflection, infrared (IR) spectroscopy, and lipid-protein interactions with FomA were characterized by using electron paramagnetic resonance (EPR) spectroscopy of spin-labeled lipids. Approximately 190 residues of membranous FomA are estimated to be in a !-sheet configuration from IR band fitting, which is consistent with a 14-strand transmembrane !-barrel structure. IR dichroism of FomA indicates that the !-strands are tilted by !45° relative to the sheet/barrel axis and that the order parameter of the latter displays a discontinuity corresponding to hydrophobic matching with fluid C(13:0) lipid chains. The stoichiometry (Nb ) 23 lipids/monomer) of lipid-protein interaction from EPR demonstrates that FomA is not trimeric in membranes of diC(14:0) phosphatidylcholine and is consistent with a monomeric !-barrel of 14-16 strands. The pronounced selectivity of interaction found with anionic spin-labeled lipids places basic residues of the protein in the vicinity of the polar-apolar membrane interfaces, consistent with current topology models. Comparison with similar data from the 8- to 22-stranded E. coli outer membrane proteins, OmpA, OmpG, and FhuA, supports the above conclusions.</dcterms:abstract>
    <dc:language>eng</dc:language>
    <dc:contributor>Marsh, Derek</dc:contributor>
    <dc:contributor>Vijay, N.</dc:contributor>
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