| Literature DB >> 22158895 |
Vitold E Galkin1, Albina Orlova, Dmitri S Kudryashov, Alexander Solodukhin, Emil Reisler, Gunnar F Schröder, Edward H Egelman.
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.Entities:
Mesh:
Substances:
Year: 2011 PMID: 22158895 PMCID: PMC3251117 DOI: 10.1073/pnas.1110109108
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205