Vitold E Galkin / Albina Orlova / Dmitri S Kudryashov / Alexander Solodukhin / Emil Reisler / Gunnar F Schröder / Edward H Egelman /
PubMed 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- ...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.
EMDB-5354: Remodeling of actin filaments by ADF-cofilin proteins PDB-3j0s: Remodeling of actin filaments by ADF cofilin proteins Method: EM (helical sym.) / Resolution: 9.0 Å
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Keywords
CONTRACTILE PROTEIN/PROTEIN BINDING / helical polymer / 
