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. 1998 Feb;74(2 Pt 1):764–772. doi: 10.1016/S0006-3495(98)74001-9

Determination of the gelsolin binding site on F-actin: implications for severing and capping.

A McGough 1, W Chiu 1, M Way 1
PMCID: PMC1302557  PMID: 9533689

Abstract

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.

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Selected References

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