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fd coat protein structure in membrane environments

P A McDonnell1, K Shon, Y Kim

  • 1Department of Chemistry, University of Pennsylvania, Philadelphia 19104.

Journal of Molecular Biology
|October 5, 1993
PubMed
Summary
This summary is machine-generated.

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The membrane-bound bacteriophage fd coat protein features two distinct helical domains, differing in arrangement and dynamics from its viral form. This study reveals its structure and mobility in lipid bilayers.

Area of Science:

  • Structural biology
  • Biophysics
  • Molecular biology

Background:

  • Bacteriophage fd coat protein exists in viral and membrane-bound forms.
  • Understanding the structural and dynamic differences is crucial for comprehending its biological function.

Purpose of the Study:

  • To characterize the secondary structure, orientation, and backbone dynamics of the membrane-bound fd coat protein.
  • To compare the membrane-bound form with the structural form found in virus particles.

Main Methods:

  • Multidimensional solution NMR on protein in micelles.
  • High-resolution solid-state NMR on protein in lipid bilayers (oriented and unoriented).

Main Results:

  • The membrane-bound fd coat protein monomer possesses a hydrophobic transmembrane helix and an amphipathic helix.

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  • Secondary structure is largely alpha-helical, similar to the viral form, but arranged perpendicularly.
  • Significant differences in residue dynamics were observed, particularly in the inter-helix turn and C-terminus, which are mobile in the membrane-bound form.

    • Conclusions:

    • The membrane-bound fd coat protein adopts a unique two-helix arrangement distinct from its viral counterpart.
    • The observed mobility in specific regions suggests functional implications for membrane interaction.
    • NMR techniques effectively elucidated the structure and dynamics of the protein in different environments.