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Yorodumi- PDB-3aae: Crystal structure of Actin capping protein in complex with CARMIL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3aae | ||||||
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Title | Crystal structure of Actin capping protein in complex with CARMIL fragment | ||||||
Components |
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Keywords | PROTEIN BINDING / ACTIN CAPPING PROTEIN / BARBED END REGULATION / CARMIL FAMILY PROTEIN / CONFORMATIONAL CHANGE / CELL MOTILITY / Actin capping / Actin-binding / Cytoskeleton / Isopeptide bond / Leucine-rich repeat | ||||||
Function / homology | Function and homology information barbed-end actin filament uncapping / positive regulation of lamellipodium organization / negative regulation of barbed-end actin filament capping / Advanced glycosylation endproduct receptor signaling / RHOD GTPase cycle / RHOF GTPase cycle / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-independent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / macropinosome ...barbed-end actin filament uncapping / positive regulation of lamellipodium organization / negative regulation of barbed-end actin filament capping / Advanced glycosylation endproduct receptor signaling / RHOD GTPase cycle / RHOF GTPase cycle / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-independent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / macropinosome / Factors involved in megakaryocyte development and platelet production / actin filament network formation / WASH complex / : / F-actin capping protein complex / macropinocytosis / urate metabolic process / negative regulation of filopodium assembly / regulation of Arp2/3 complex-mediated actin nucleation / Factors involved in megakaryocyte development and platelet production / cell junction assembly / ruffle organization / barbed-end actin filament capping / actin polymerization or depolymerization / regulation of cell morphogenesis / regulation of lamellipodium assembly / intermediate filament cytoskeleton / lamellipodium assembly / establishment or maintenance of cell polarity / cortical cytoskeleton / positive regulation of actin filament polymerization / filamentous actin / brush border / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of stress fiber assembly / cytoskeleton organization / hippocampal mossy fiber to CA3 synapse / Schaffer collateral - CA1 synapse / cell morphogenesis / Z disc / actin filament binding / cell migration / lamellipodium / actin cytoskeleton organization / postsynaptic density / positive regulation of cell migration / nuclear speck / protein-containing complex binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å | ||||||
Authors | Takeda, S. / Minakata, S. / Narita, A. / Kitazawa, M. / Yamakuni, T. / Maeda, Y. / Nitanai, Y. | ||||||
Citation | Journal: To be Published Title: Two distinct mechanisms for the regulation of actin capping protein-competitive or allosteric inhibitions Authors: Takeda, S. / Minakata, S. / Narita, A. / Kitazawa, M. / Yamakuni, T. / Maeda, Y. / Nitanai, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3aae.cif.gz | 536.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3aae.ent.gz | 444.7 KB | Display | PDB format |
PDBx/mmJSON format | 3aae.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3aae_validation.pdf.gz | 550.3 KB | Display | wwPDB validaton report |
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Full document | 3aae_full_validation.pdf.gz | 595.8 KB | Display | |
Data in XML | 3aae_validation.xml.gz | 92 KB | Display | |
Data in CIF | 3aae_validation.cif.gz | 124.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aa/3aae ftp://data.pdbj.org/pub/pdb/validation_reports/aa/3aae | HTTPS FTP |
-Related structure data
Related structure data | 3aa0S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
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Details | THE ORIGOMETRIC STATE OF THE ACTIN CAPPING PROTEIN IS A HETERO DIMER COMPOSE OF SUBUNIT A (CHAIN A) AND SUBUNIT B (CHAIN B) IN VIVO AND IN VITRO. |
-Components
#1: Protein | Mass: 33001.789 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Gene: CAPZA1 / Plasmid: PETDUET1 / Production host: Escherichia coli (E. coli) / Strain (production host): ROSETTA2 (DE3) / References: UniProt: P13127 #2: Protein | Mass: 31403.449 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Gene: CAPZB / Plasmid: PETDUET1 / Production host: Escherichia coli (E. coli) / Strain (production host): ROSETTA2 (DE3) / References: UniProt: P14315 #3: Protein/peptide | Mass: 4167.751 Da / Num. of mol.: 5 / Fragment: CP-BINDING MOTIF, residues 971-1002 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Lrrc16a / Plasmid: PGEX6P1 / Production host: Escherichia coli (E. coli) / Strain (production host): ROSETTA2 (DE3) / References: UniProt: Q6EDY6 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.12 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 14% PEG 3350, 180MM TRI-AMMONIUM CITRATE, 100MM MES-NAOH, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44B2 / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 4r / Detector: CCD / Date: Apr 23, 2008 / Details: mirrors |
Radiation | Monochromator: SI / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→49.7 Å / Num. obs: 58413 / % possible obs: 99.5 % / Redundancy: 7.6 % / Biso Wilson estimate: 38.1 Å2 / Rmerge(I) obs: 0.126 / Net I/σ(I): 16.4 |
Reflection shell | Resolution: 3.3→3.42 Å / Redundancy: 7.7 % / Rmerge(I) obs: 0.382 / Mean I/σ(I) obs: 5.56 / Num. unique all: 5823 / % possible all: 99.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3AA0 Resolution: 3.3→49.7 Å / Cor.coef. Fo:Fc: 0.869 / Cor.coef. Fo:Fc free: 0.843 / Occupancy max: 1 / Occupancy min: 1 / SU B: 27.301 / SU ML: 0.45 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.576 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 99.82 Å2 / Biso mean: 50.947 Å2 / Biso min: 27.63 Å2
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Refine analyze | Luzzati coordinate error obs: 0.67 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.3→49.7 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION
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