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Yorodumi- PDB-5v6e: Crystal structure of Myosin VI in complex with GH2 domain of GIPC1 -
+Open data
-Basic information
Entry | Database: PDB / ID: 5v6e | |||||||||
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Title | Crystal structure of Myosin VI in complex with GH2 domain of GIPC1 | |||||||||
Components |
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Keywords | PROTEIN BINDING / helical bundle | |||||||||
Function / homology | Function and homology information FGFR1b ligand binding and activation / FGFR1c ligand binding and activation / RHOBTB1 GTPase cycle / presynaptic endocytic zone / RHOU GTPase cycle / RHOBTB2 GTPase cycle / Gap junction degradation / cochlear hair cell ribbon synapse / regulation of secretion / Trafficking of AMPA receptors ...FGFR1b ligand binding and activation / FGFR1c ligand binding and activation / RHOBTB1 GTPase cycle / presynaptic endocytic zone / RHOU GTPase cycle / RHOBTB2 GTPase cycle / Gap junction degradation / cochlear hair cell ribbon synapse / regulation of secretion / Trafficking of AMPA receptors / cellular response to electrical stimulus / positive regulation of melanin biosynthetic process / postsynaptic neurotransmitter receptor internalization / inner ear auditory receptor cell differentiation / postsynaptic actin cytoskeleton / vesicle membrane / glutamate secretion / vesicle transport along actin filament / cellular response to interleukin-7 / myosin complex / clathrin-coated vesicle / microfilament motor activity / inner ear morphogenesis / myosin binding / dendrite development / positive regulation of transforming growth factor beta receptor signaling pathway / positive regulation of cytokinesis / filamentous actin / inner ear development / microvillus / brush border / endocytic vesicle / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / DNA damage response, signal transduction by p53 class mediator / protein targeting / endothelial cell migration / clathrin-coated pit / ruffle / synapse assembly / presynaptic modulation of chemical synaptic transmission / GTPase activator activity / dendritic shaft / locomotory behavior / filopodium / actin filament organization / PDZ domain binding / sensory perception of sound / regulation of synaptic plasticity / Schaffer collateral - CA1 synapse / regulation of protein stability / ruffle membrane / endocytosis / actin filament binding / synaptic vesicle / actin cytoskeleton / protein transport / presynapse / apical part of cell / actin binding / cell cortex / chemical synaptic transmission / cytoplasmic vesicle / postsynapse / nuclear membrane / dendritic spine / postsynaptic density / calmodulin binding / response to xenobiotic stimulus / G protein-coupled receptor signaling pathway / axon / signaling receptor binding / neuronal cell body / glutamatergic synapse / synapse / perinuclear region of cytoplasm / Golgi apparatus / protein-containing complex / nucleoplasm / ATP binding / membrane / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.506 Å | |||||||||
Authors | Shang, G. / Zhang, X. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Elife / Year: 2017 Title: Structure analyses reveal a regulated oligomerization mechanism of the PlexinD1/GIPC/myosin VI complex. Authors: Shang, G. / Brautigam, C.A. / Chen, R. / Lu, D. / Torres-Vazquez, J. / Zhang, X. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5v6e.cif.gz | 249.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5v6e.ent.gz | 207.3 KB | Display | PDB format |
PDBx/mmJSON format | 5v6e.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v6/5v6e ftp://data.pdbj.org/pub/pdb/validation_reports/v6/5v6e | HTTPS FTP |
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-Related structure data
Related structure data | 5v6bC 5v6hSC 5v6rC 5v6tC C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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5 |
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Unit cell |
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-Components
#1: Protein | Mass: 8962.971 Da / Num. of mol.: 5 / Fragment: UNP residues 258-333 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Gipc1, Gipc, Rgs19ip1, Semcap1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Z0G0 #2: Protein/peptide | Mass: 5786.563 Da / Num. of mol.: 5 / Fragment: UNP residues 1055-1099 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Myo6, Sv / Production host: Escherichia coli (E. coli) / References: UniProt: Q64331 |
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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: 5.49 Å3/Da / Density % sol: 77.61 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1 M Bis-Tris pH 6.0 and 2 M (NH4)2SO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9794 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 15, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→50 Å / Num. obs: 20339 / % possible obs: 97 % / Redundancy: 6.1 % / Rpim(I) all: 0.074 / Net I/σ(I): 10.3 |
Reflection shell | Resolution: 3.5→3.56 Å / Redundancy: 6 % / Rpim(I) all: 0.493 / % possible all: 97 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5V6H Resolution: 3.506→47.082 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.49 / Phase error: 22.45 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.506→47.082 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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