+Open data
-Basic information
Entry | Database: PDB / ID: 3j0s | ||||||
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Title | Remodeling of actin filaments by ADF cofilin proteins | ||||||
Components |
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Keywords | CONTRACTILE PROTEIN/PROTEIN BINDING / helical polymer / CONTRACTILE PROTEIN-ACTIN BINDING PROTEIN complex / CONTRACTILE PROTEIN-PROTEIN BINDING complex | ||||||
Function / homology | Function and homology information Gap junction degradation / Formation of annular gap junctions / RHO GTPases activate IQGAPs / DNA Damage Recognition in GG-NER / Adherens junctions interactions / Clathrin-mediated endocytosis / UCH proteinases / RHO GTPases Activate Formins / actin filament fragmentation / positive regulation of embryonic development ...Gap junction degradation / Formation of annular gap junctions / RHO GTPases activate IQGAPs / DNA Damage Recognition in GG-NER / Adherens junctions interactions / Clathrin-mediated endocytosis / UCH proteinases / RHO GTPases Activate Formins / actin filament fragmentation / positive regulation of embryonic development / establishment of spindle localization / EPH-ephrin mediated repulsion of cells / structural constituent of postsynaptic actin cytoskeleton / dense body / EPHB-mediated forward signaling / VEGFA-VEGFR2 Pathway / actin filament severing / regulation of dendritic spine morphogenesis / positive regulation by host of viral process / actin filament depolymerization / RHO GTPases Activate ROCKs / regulation of cell morphogenesis / NuA4 histone acetyltransferase complex / lamellipodium membrane / Rho protein signal transduction / Sema3A PAK dependent Axon repulsion / mitotic cytokinesis / cytoskeleton organization / EPHB-mediated forward signaling / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / axonogenesis / actin filament / cell motility / ruffle membrane / response to virus / Regulation of actin dynamics for phagocytic cup formation / nuclear matrix / actin filament binding / actin cytoskeleton / Platelet degranulation / lamellipodium / growth cone / actin cytoskeleton organization / vesicle / cytoskeleton / axon / focal adhesion / synapse / negative regulation of apoptotic process / protein kinase binding / extracellular space / extracellular exosome / ATP binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Gallus gallus (chicken) | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 9 Å | ||||||
Authors | Galkin, V.E. / Orlova, A. / Kudryashov, D.S. / Solodukhin, A. / Reisler, E. / Schroeder, G.F. / Egelman, E.H. | ||||||
Citation | 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. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
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PDBx/mmCIF format | 3j0s.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb3j0s.ent.gz | 852.8 KB | Display | PDB format |
PDBx/mmJSON format | 3j0s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3j0s_validation.pdf.gz | 828.2 KB | Display | wwPDB validaton report |
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Full document | 3j0s_full_validation.pdf.gz | 864.4 KB | Display | |
Data in XML | 3j0s_validation.xml.gz | 126.7 KB | Display | |
Data in CIF | 3j0s_validation.cif.gz | 192.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j0/3j0s ftp://data.pdbj.org/pub/pdb/validation_reports/j0/3j0s | HTTPS FTP |
-Related structure data
Related structure data | 5354MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Details | 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 |
-Components
#1: Protein | 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 | 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 | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
-Sample preparation
Component | Name: actin decorated with cofilin / Type: COMPLEX / Details: filament containing one cofilin to one actin |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK I / Cryogen name: ETHANE / Humidity: 100 % |
-Electron microscopy imaging
Experimental equipment | Model: Tecnai F20 / Image courtesy: FEI Company |
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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 |
Specimen holder | Specimen holder model: GATAN LIQUID NITROGEN / Specimen holder type: SIDE ENTRY |
Image recording | Film or detector model: KODAK SO-163 FILM |
Image scans | Num. digital images: 125 |
-Processing
Software |
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EM software |
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CTF correction | Details: each EM | ||||||||||||
Helical symmerty | Angular rotation/subunit: 162.1 ° / Axial rise/subunit: 27.6 Å / Axial symmetry: C1 | ||||||||||||
3D reconstruction | Method: IHRSR / Resolution: 9 Å / Resolution method: FSC / Symmetry type: HELICAL | ||||||||||||
Atomic model building | Space: REAL | ||||||||||||
Refinement step | Cycle: LAST
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