Journal: Proc Natl Acad Sci U S A / Year: 2011 Title: Remodeling of actin filaments by ADF/cofilin proteins. Authors: Vitold E Galkin / 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- ...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.
THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR HELICAL SYMMETRY WITH THE FOLLOWING PARAMETERS: ROTATION PER SUBUNIT (TWIST) = -162.1 DEGREES; RISE PER SUBUNIT (HEIGHT) = 27.6 ANGSTROM
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Components
#1: Protein
Actin, cytoplasmic1 / Beta-actin
Mass: 41651.465 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / Tissue: muscle / References: UniProt: P60706
#2: Protein
Cofilin-2 / Cofilin / muscle isoform
Mass: 18532.531 Da / Num. of mol.: 12 / Fragment: SEE REMARK 999 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CFL1, CFL / Production host: Escherichia coli (E. coli) / References: UniProt: P23528*PLUS
Sequence details
THE AUTHORS STATE THAT HUMAN COFILIN-2 WAS USED IN THE EXPERIMENT, BUT HUMAN COFILIN-1 (UNP P23528) ...THE AUTHORS STATE THAT HUMAN COFILIN-2 WAS USED IN THE EXPERIMENT, BUT HUMAN COFILIN-1 (UNP P23528) WAS USED FOR MODELING.
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Experimental details
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Experiment
Experiment
Method: ELECTRON MICROSCOPY
EM experiment
Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction
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Sample preparation
Component
Name: actin decorated with cofilin / Type: COMPLEX / Details: filament containing one cofilin to one actin
Specimen
Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Vitrification
Instrument: FEI VITROBOT MARK I / Cryogen name: ETHANE / Humidity: 100 %
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Electron microscopy imaging
Experimental equipment
Model: Tecnai F20 / Image courtesy: FEI Company
Microscopy
Model: FEI TECNAI F20 / Date: Jan 1, 2010
Electron gun
Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lens
Mode: BRIGHT FIELD / Nominal magnification: 50000 X / Nominal defocus max: 5300 nm / Nominal defocus min: 1100 nm / Cs: 2 mm
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