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Related Experiment Videos

Three-dimensional solution structure of Acanthamoeba profilin-I

V K Vinson1, S J Archer, E E Lattman

  • 1Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.

The Journal of Cell Biology
|September 1, 1993
PubMed
Summary

We determined the 3D structure of Acanthamoeba profilin-I, revealing distinct faces for actin and lipid binding. This provides insights into the protein's molecular interactions and functional differences between isoforms.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Profilins are actin-binding proteins crucial for cytoskeleton regulation.
  • Acanthamoeba profilin-I and II exhibit differences in polyphosphoinositide binding.
  • Understanding profilin structure is key to elucidating its diverse cellular roles.

Purpose of the Study:

  • To determine the three-dimensional solution structure of Acanthamoeba profilin-I.
  • To identify the molecular regions involved in actin and lipid binding.
  • To understand the structural basis for differential polyphosphoinositide binding between profilin isoforms.

Main Methods:

  • Multidimensional nuclear magnetic resonance (NMR) spectroscopy was employed to determine the protein structure.
  • Actin-profilin cross-linking experiments were conducted.

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  • Localization of conserved residues across different phyla was analyzed.

    • Main Results:

    • A medium-resolution 3D structure of Acanthamoeba profilin-I was established.
    • The protein comprises a five-stranded antiparallel beta sheet with flanking helices and additional beta strands.
    • Actin binding is localized to the face with terminal helices, while the opposite face shows isoform-specific residues potentially involved in lipid binding.

    Conclusions:

    • Actin and lipids bind to distinct faces of Acanthamoeba profilin-I.
    • The structural differences on one face explain the varying polyphosphoinositide binding affinities of profilin isoforms.
    • This study provides a structural framework for understanding profilin's dual role in actin and lipid interactions.