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Domain motions in actin

R Page1, U Lindberg, C E Schutt

  • 1Henry H. Hoyt Laboratory, Princeton University, Princeton, NJ, 08544, USA.

Journal of Molecular Biology
|July 17, 1998
PubMed
Summary

Actin undergoes conformational changes through shear motion at the interface between its two rigid cores. Small rotations in connecting residues allow for structural transitions while maintaining domain integrity.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Actin's large conformational changes are well-documented, even when bound to actin-binding proteins.
  • Previous studies suggested domain rotation mechanisms, but a detailed classification was lacking.

Purpose of the Study:

  • To formally analyze domain motions in actin using available crystal structures.
  • To classify actin's conformational change mechanism as hinge or shear and quantify its magnitude.

Main Methods:

  • Formal analysis of domain motions in four actin crystal structures.
  • Application of an algorithm for identifying protein hinges to analyze residue movements.
  • Quantification of torsion angle changes in connecting polypeptides.

Main Results:

  • Actin comprises two rigid cores, a semi-rigid domain, and three flexible loops.
  • Residues at the interface between rigid cores exhibit shear motion between conformations.
  • Small torsion angle rotations (<7 degrees) in five residues facilitate conformational transitions.
  • Actin secondary structures remain conformationally invariant across different complexes.
  • Current F-actin models are inconsistent with identified actin conformational principles.

Conclusions:

  • Actin conformational changes are primarily driven by shear at the inter-core interface.
  • The identified mechanism explains how actin maintains domain integrity during structural transitions.
  • Findings necessitate re-evaluation of current F-actin models.

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