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Yorodumi- PDB-3v00: Studies of a constitutively active G-alpha subunit provide insigh... -
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-Basic information
Entry | Database: PDB / ID: 3v00 | ||||||
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Title | Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. | ||||||
Components | Guanine nucleotide-binding protein G(t) subunit alpha-1/ Guanine nucleotide-binding protein G(i) subunit alpha-1 chimeric protein | ||||||
Keywords | SIGNALING PROTEIN / GTPase / GTP binding / Transducer / SIGNAL TRANSDUCTION / CELL CYCLE | ||||||
Function / homology | Function and homology information Extra-nuclear estrogen signaling / Adenylate cyclase inhibitory pathway / detection of light stimulus involved in visual perception / negative regulation of cyclic-nucleotide phosphodiesterase activity / G protein-coupled receptor complex / Inactivation, recovery and regulation of the phototransduction cascade / Activation of the phototransduction cascade / phototransduction, visible light / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 ...Extra-nuclear estrogen signaling / Adenylate cyclase inhibitory pathway / detection of light stimulus involved in visual perception / negative regulation of cyclic-nucleotide phosphodiesterase activity / G protein-coupled receptor complex / Inactivation, recovery and regulation of the phototransduction cascade / Activation of the phototransduction cascade / phototransduction, visible light / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / GTPase activating protein binding / negative regulation of synaptic transmission / G alpha (i) signalling events / neurotransmitter receptor localization to postsynaptic specialization membrane / photoreceptor outer segment membrane / G alpha (i) signalling events / phototransduction / response to light stimulus / acyl binding / D2 dopamine receptor binding / positive regulation of protein localization to cell cortex / regulation of cAMP-mediated signaling / G protein-coupled serotonin receptor binding / cellular response to forskolin / regulation of mitotic spindle organization / photoreceptor inner segment / G protein-coupled receptor binding / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / photoreceptor disc membrane / GDP binding / heterotrimeric G-protein complex / cell cortex / midbody / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / postsynapse / G protein-coupled receptor signaling pathway / cell division / GTPase activity / centrosome / glutamatergic synapse / GTP binding / protein kinase binding / magnesium ion binding / protein-containing complex / nucleus / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å | ||||||
Authors | Singh, G. / Cerione, R.A. | ||||||
Citation | Journal: Biochemistry / Year: 2012 Title: A constitutively active G-alpha subunit provide insights into the mechanism of G protein activation Authors: Singh, G. / Ramachandran, S. / Cerione, R.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3v00.cif.gz | 228.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3v00.ent.gz | 183.8 KB | Display | PDB format |
PDBx/mmJSON format | 3v00.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3v00_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 3v00_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 3v00_validation.xml.gz | 46.3 KB | Display | |
Data in CIF | 3v00_validation.cif.gz | 63.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v0/3v00 ftp://data.pdbj.org/pub/pdb/validation_reports/v0/3v00 | HTTPS FTP |
-Related structure data
Related structure data | 1tagS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
-Components
#1: Protein | Mass: 40999.656 Da / Num. of mol.: 3 / Fragment: UNP P04695 1-215 & 295-350, UNP P10824 220-298 / Mutation: G56P, K244H and D247N Source method: isolated from a genetically manipulated source Details: T7 LAC PROMOTER Source: (gene. exp.) Bos taurus (cattle), (gene. exp.) Rattus norvegicus (Norway rat) Gene: GNAT1, GNAT1_BOVIN / Plasmid: PET VECTOR / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P04695, UniProt: P10824 #2: Chemical | #3: Water | ChemComp-HOH / | |
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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: 3.36 Å3/Da / Density % sol: 63.39 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.3 Details: 1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.978 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Nov 8, 2007 / Details: Mirrors |
Radiation | Monochromator: Horizontal focusing 5.05 asymmetric cut Si(111) Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→39.74 Å / Num. all: 47386 / Num. obs: 47006 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 11.3 / Redundancy: 8.6 % / Biso Wilson estimate: 89.2 Å2 / Rmerge(I) obs: 0.08 / Rsym value: 0.08 / Net I/σ(I): 21.253 |
Reflection shell | Resolution: 2.7→2.8 Å / % possible all: 8.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1TAG Resolution: 2.9→39.74 Å / Rfactor Rfree error: 0.005 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Displacement parameters | Biso mean: 94.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error free: 0.46 Å / Luzzati sigma a free: 0.56 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→39.74 Å
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Refine LS restraints |
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