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Biophys J, February 1998, p. 764-772, Vol. 74, No. 2

Determination of the Gelsolin Binding Site on F-actin: Implications for Severing and Capping

Amy McGough,* Wah Chiu,* and Michael Way#

 *Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030 USA, and  #European Molecular Biology Laboratory, 69117 Heidelberg, Germany

Gelsolin is a six-domain protein that regulates actin assembly by severing, capping, and nucleating filaments. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on F-actin. To obtain fully decorated filaments under severing conditions, we have studied a derivative (G2-6) that has a reduced severing efficiency compared to gelsolin. A three-dimensional reconstruction of G2-6:F-actin was obtained by electron cryomicroscopy and helical reconstruction. The structure shows that gelsolin bridges two longitudinally associated monomers when it binds the filament. The F-actin binding region of G2-6 is centered axially at subdomain 3 and radially between subdomains 1 and 3 of the upper actin monomer. Our results suggest that for severing to occur, both gelsolin and actin undergo large conformational changes.

Biophys J, February 1998, p. 764-772, Vol. 74, No. 2
© 1998 by the Biophysical Society   0006-3495/98/02/764/09  $2.00


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