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A liquid diffraction analysis of sarcoplasmic reticulum. I. Compositional variation.

G W Brady, D B Fein, M E Harder

    Biophysical Journal
    |April 1, 1981
    PubMed
    Summary
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    X-ray scattering reveals the structure of sarcoplasmic reticulum (SR) proteins. Rabbit muscle SR ATPase is monomeric and asymmetrically embedded in the lipid bilayer.

    Area of Science:

    • Biophysics
    • Structural Biology
    • Membrane Protein Analysis

    Background:

    • Sarcoplasmic reticulum (SR) is crucial for muscle contraction, storing and releasing calcium ions.
    • The Mg++-dependent, Ca++-stimulated ATPase (SERCA) is the primary protein in SR membranes, responsible for calcium transport.
    • Understanding the structure and membrane interactions of SERCA is key to elucidating muscle function.

    Purpose of the Study:

    • To determine the structural characteristics of the ATPase protein within the sarcoplasmic reticulum membrane.
    • To analyze the interactions between ATPase and the surrounding lipid bilayer.
    • To investigate the transbilayer disposition of the ATPase molecule.

    Main Methods:

    • X-ray scattering intensity measurements on fragmented rabbit muscle SR samples.

    Related Experiment Videos

  • Analysis of scattering data using methods for binary liquid mixtures.
  • Determination of the pair correlation function to assess protein-lipid interactions.

    • Main Results:

    • Identified separable contributions of protein, lipid, and their interactions to the scattering profiles.
    • The protein scattering profile suggests a monomeric ATPase particle with dimensions of 142 Å length and 35 Å diameter.
    • Analysis indicates a fully asymmetric disposition of the ATPase within the lipid bilayer.

    Conclusions:

    • The dominant ATPase species in rabbit muscle SR is monomeric.
    • The ATPase molecule exhibits a highly asymmetric orientation within the lipid bilayer, with one end interfacing with either the lumenal or cytoplasmic surface.