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Crystalline actin sheets: their structure and polymorphism

U Aebi, W E Fowler, G Isenberg

    The Journal of Cell Biology
    |November 1, 1981
    PubMed
    Summary
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    Gadolinium-induced crystalline sheets of Acanthamoeba actin reveal three polymorphic forms. These structures provide a novel model for actin molecule research and protein binding studies.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Microscopy

    Background:

    • Actin is a crucial protein involved in cell structure and motility.
    • Understanding actin's structure is key to deciphering its various cellular functions.
    • Previous studies on actin structure have primarily focused on actin filaments.

    Purpose of the Study:

    • To characterize the polymorphic forms of Acanthamoeba actin crystalline sheets induced by gadolinium.
    • To determine the three-dimensional model of the actin molecule using electron microscopy.
    • To investigate the potential of these sheets for studying actin-binding proteins.

    Main Methods:

    • Induction of crystalline actin sheets using gadolinium.
    • Electron microscopy for imaging sheet structures.

    Related Experiment Videos

  • Image processing and analysis to generate a molecular model.
  • Determination of actin monomer packing symmetry.

    • Main Results:

    • Identified three distinct polymorphic forms: rectangular sheets, square sheets, and cylinders.
    • Developed a projection model of the actin molecule at 1.5 nm resolution.
    • Observed actin molecule dimensions of 5.6 x 3.3 x 4.5 nm with a bilobed structure.
    • Determined that actin monomers are arranged with P2 symmetry in the sheets, differing from filament packing.

    Conclusions:

    • Gadolinium-induced actin sheets exhibit unique polymorphic forms and packing arrangements.
    • The derived actin molecule model offers new insights into its structure.
    • The exposed surface area of actin in these sheets facilitates the study of actin-binding protein interactions.