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- PDB-3m3n: Structure of a Longitudinal Actin Dimer Assembled by Tandem W Domains -
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Basic information
Entry | Database: PDB / ID: 3m3n | ||||||
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Title | Structure of a Longitudinal Actin Dimer Assembled by Tandem W Domains | ||||||
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![]() | STRUCTURAL PROTEIN / actin dimer / ATP-binding / actin cytoskeleton / methylation / muscle protein / actin-binding / MOTOR PROTEIN | ||||||
Function / homology | ![]() negative regulation of membrane tubulation / spindle localization / membrane invagination / positive regulation of clathrin-dependent endocytosis / plasma membrane tubulation / negative regulation of lymphocyte migration / postsynapse organization / actin nucleation / positive regulation of smooth muscle cell differentiation / regulation of cell projection assembly ...negative regulation of membrane tubulation / spindle localization / membrane invagination / positive regulation of clathrin-dependent endocytosis / plasma membrane tubulation / negative regulation of lymphocyte migration / postsynapse organization / actin nucleation / positive regulation of smooth muscle cell differentiation / regulation of cell projection assembly / actin cap / vesicle organization / postsynaptic actin cytoskeleton organization / sequestering of actin monomers / Platelet degranulation / vesicle transport along actin filament / vesicle budding from membrane / positive regulation of chemotaxis / protein-containing complex localization / dendritic spine morphogenesis / positive regulation of filopodium assembly / regulation of postsynapse organization / cytoskeletal motor activator activity / tropomyosin binding / mesenchyme migration / positive regulation of smooth muscle cell migration / troponin I binding / myosin heavy chain binding / cell leading edge / filamentous actin / actin filament bundle / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / cytoskeletal protein binding / regulation of cell migration / actin filament polymerization / filopodium / actin filament organization / actin filament / response to bacterium / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / regulation of protein localization / lamellipodium / actin binding / cell body / actin cytoskeleton organization / cytoplasmic vesicle / postsynapse / cytoskeleton / hydrolase activity / protein domain specific binding / cell division / Golgi membrane / glutamatergic synapse / calcium ion binding / positive regulation of gene expression / positive regulation of DNA-templated transcription / magnesium ion binding / positive regulation of transcription by RNA polymerase II / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rebowski, G. / Namgoong, S. / Dominguez, R. | ||||||
![]() | ![]() Title: Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation. Authors: Rebowski, G. / Namgoong, S. / Boczkowska, M. / Leavis, P.C. / Navaza, J. / Dominguez, R. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 161.5 KB | Display | ![]() |
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PDB format | ![]() | 126.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3m1fSC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 41875.633 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | | Mass: 11094.438 Da / Num. of mol.: 1 / Fragment: Engineered tandem W domain construct 3W Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Chemical | #4: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.54 Å3/Da / Density % sol: 65.29 % |
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Crystal grow | Temperature: 300 K / pH: 10 Details: 100 mM CAPS pH 10.0, and 24% PEG 3350, 100 mM RbCl, VAPOR DIFFUSION, HANGING DROP, temperature 300.0K |
-Data collection
Diffraction | Mean temperature: 112 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Jul 23, 2009 Details: CYLINDRICALLY BENT ULE GLASS MIRROR WITH PT AND PD COATINGS |
Radiation | Monochromator: CRYOGENICALLY-COOLED SI(111) DOUBLE-CRYSTAL SYSTEM Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 7→50 Å / Num. obs: 2182 / % possible obs: 90 % / Redundancy: 20.5 % / Rmerge(I) obs: 0.086 / Net I/σ(I): 16.5 |
Reflection shell | Resolution: 7→7.25 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.389 / Mean I/σ(I) obs: 1 / % possible all: 34.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3M1F Resolution: 7→50 Å / Details: NO REFINEMENT WAS PERFORMED | ||||||||||||||
Refinement step | Cycle: LAST / Resolution: 7→50 Å
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