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Nature. 2009 Jan 22;457(7228):441-5. doi: 10.1038/nature07685.

The nature of the globular- to fibrous-actin transition.

Author information

1
X-ray Structural Analysis Research Team, RIKEN SPring-8 Center, RIKEN Harima Institute, 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan. toda@spring8.or.jp

Erratum in

  • Nature. 2009 Sep 24;461(7263):550.

Abstract

Actin plays crucial parts in cell motility through a dynamic process driven by polymerization and depolymerization, that is, the globular (G) to fibrous (F) actin transition. Although our knowledge about the actin-based cellular functions and the molecules that regulate the G- to F-actin transition is growing, the structural aspects of the transition remain enigmatic. We created a model of F-actin using X-ray fibre diffraction intensities obtained from well oriented sols of rabbit skeletal muscle F-actin to 3.3 A in the radial direction and 5.6 A along the equator. Here we show that the G- to F-actin conformational transition is a simple relative rotation of the two major domains by about 20 degrees. As a result of the domain rotation, the actin molecule in the filament is flat. The flat form is essential for the formation of stable, helical F-actin. Our F-actin structure model provides the basis for understanding actin polymerization as well as its molecular interactions with actin-binding proteins.

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PMID:
19158791
DOI:
10.1038/nature07685
[Indexed for MEDLINE]

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