Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20568-72. Epub 2011 Dec 7.

Remodeling of actin filaments by ADF/cofilin proteins.

Galkin VE, Orlova A, Kudryashov DS, Solodukhin A, Reisler E, Schröder GF, Egelman EH.

Source

Department of Biochemistry and Molecular Genetics, University of Virginia, Box 800733, Charlottesville, VA 22908-0733, USA. galkin@virginia.edu

Abstract

Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.

PMID:: 22158895; [PubMed - in process]
PMCID:: PMC3251117; [Available on 2012/6/20]

Publication Types, Secondary Source ID, Grant Support

Publication Types

Research Support, N.I.H., Extramural

Secondary Source ID

PDB/3J0S

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Structures reported by this article

Remodeling Of Actin Filaments By Adf Cofilin Proteins

PDB: 3J0S

Source: Gallus gallus, Homo sapiens

Method: Electron Microscopy

Resolution: 9 Å

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