Determination of the Gelsolin Binding Site on F-actin: Implications for Severing and Capping
| Autor: | Amy McGough, Wah Chiu, Michael Way |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Cryo-electron microscopy Biophysics macromolecular substances Protein Structure Secondary Protein filament chemistry.chemical_compound Protein structure Freezing Escherichia coli Image Processing Computer-Assisted Binding site Cloning Molecular Actin Gelsolin Binding Sites Chemistry Microfilament Proteins Microfilament Protein Actins Recombinant Proteins Crystallography Microscopy Electron Monomer Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0006-3495 |
| DOI: | 10.1016/s0006-3495(98)74001-9 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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