3J0S

Remodeling of actin filaments by ADF cofilin proteins

Summary for 3J0S

• Entry DOI: 10.2210/pdb3j0s/pdb
• EMDB information: 5354
• Descriptor: Actin, cytoplasmic 1, Cofilin-2 (2 entities in total)
• Functional Keywords: helical polymer, contractile protein-actin binding protein complex, contractile protein-protein binding complex, contractile protein/protein binding
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 24
• Total formula weight: 722207.95

Authors

Galkin, V.E.,Orlova, A.,Kudryashov, D.S.,Solodukhin, A.,Reisler, E.,Schroeder, G.F.,Egelman, E.H. (deposition date: 2011-11-24, release date: 2011-12-21, Last modification date: 2024-02-21)

Primary citation

Galkin, V.E.,Orlova, A.,Kudryashov, D.S.,Solodukhin, A.,Reisler, E.,Schroder, G.F.,Egelman, E.H.
Remodeling of actin filaments by ADF/cofilin proteins.
Proc.Natl.Acad.Sci.USA, 108:20568-20572, 2011

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-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.

PubMed: 22158895
DOI: 10.1073/pnas.1110109108

Experimental method

ELECTRON MICROSCOPY (9 Å)