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- PDB-3qi2: A Galpha P-loop mutation prevents transition to the activated sta... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3qi2 | ||||||
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Title | A Galpha P-loop mutation prevents transition to the activated state: G42R bound to RGS14 GoLoco | ||||||
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![]() | SIGNALING PROTEIN / RGS14 GoLoco / Ras-like domain / all-helical domain / GoLoco motif / arginine finger / lipoprotein / transducer / guanine nucleotide dissociation inhibitor / GTP binding / nucleotide binding / ADP-ribosylation | ||||||
Function / homology | ![]() zygote asymmetric cell division / negative regulation of synaptic plasticity / negative regulation of G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway / GTPase activating protein binding / GDP-dissociation inhibitor activity / nucleocytoplasmic transport / positive regulation of neurogenesis / spindle organization / platelet-derived growth factor receptor signaling pathway ...zygote asymmetric cell division / negative regulation of synaptic plasticity / negative regulation of G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway / GTPase activating protein binding / GDP-dissociation inhibitor activity / nucleocytoplasmic transport / positive regulation of neurogenesis / spindle organization / platelet-derived growth factor receptor signaling pathway / G-protein alpha-subunit binding / Adenylate cyclase inhibitory pathway / positive regulation of protein localization to cell cortex / regulation of cAMP-mediated signaling / D2 dopamine receptor binding / G protein-coupled serotonin receptor binding / long-term memory / regulation of mitotic spindle organization / cellular response to forskolin / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / GTPase activator activity / negative regulation of MAP kinase activity / learning / Regulation of insulin secretion / chromosome segregation / G protein-coupled receptor binding / long-term synaptic potentiation / G-protein beta/gamma-subunit complex binding / visual learning / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / negative regulation of ERK1 and ERK2 cascade / ADP signalling through P2Y purinoceptor 12 / PML body / response to peptide hormone / Adrenaline,noradrenaline inhibits insulin secretion / spindle pole / G alpha (z) signalling events / spindle / ADORA2B mediated anti-inflammatory cytokines production / GPER1 signaling / GDP binding / heterotrimeric G-protein complex / signaling receptor complex adaptor activity / mitotic cell cycle / cell cortex / midbody / G alpha (i) signalling events / G alpha (s) signalling events / microtubule binding / microtubule / response to oxidative stress / dendritic spine / Extra-nuclear estrogen signaling / postsynaptic density / nuclear body / cell cycle / G protein-coupled receptor signaling pathway / lysosomal membrane / cell division / GTPase activity / centrosome / glutamatergic synapse / dendrite / nucleolus / GTP binding / protein kinase binding / magnesium ion binding / extracellular exosome / nucleoplasm / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bosch, D.E. / Willard, F.S. / Kimple, A.J. / Miley, M.J. / Siderovski, D.P. | ||||||
![]() | ![]() Title: A P-loop Mutation in Galpha Subunits Prevents Transition to the Active State: Implications for G-protein Signaling in Fungal Pathogenesis Authors: Bosch, D.E. / Willard, F.S. / Ramanujam, R. / Kimple, A.J. / Willard, M.D. / Naqvi, N.I. / Siderovski, D.P. #1: ![]() Title: Structure-based protocol for identifying mutations that enhance protein-protein binding affinities. Authors: Sammond, D.W. / Eletr, Z.M. / Purbeck, C. / Kimple, R.J. / Siderovski, D.P. / Kuhlman, B. #2: ![]() Title: Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits. Authors: Kimple, R.J. / Kimple, M.E. / Betts, L. / Sondek, J. / Siderovski, D.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 283.8 KB | Display | ![]() |
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PDB format | ![]() | 230.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 27.3 KB | Display | |
Data in CIF | ![]() | 35.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3qe0C ![]() 2om2S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein / Protein/peptide , 2 types, 4 molecules ABCD
#1: Protein | Mass: 37531.750 Da / Num. of mol.: 2 / Fragment: alpha-i1 subunit, residues 31-354 / Mutation: G42R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 4093.621 Da / Num. of mol.: 2 / Fragment: GoLoco motif peptide, residues 497-532 / Source method: obtained synthetically Details: synthetic GoLoco motif peptide identical to human RGS14 497-532 References: UniProt: O43566 |
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-Non-polymers , 4 types, 42 molecules ![](data/chem/img/GDP.gif)
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#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-GOL / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.07 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5 Details: Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (10 mM Tris pH 7.5, 1 mM magnesium chloride, 5% (w/v) glycerol, 5 mM DTT) and well solution (1.7 M ammonium sulfate, 100 ...Details: Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (10 mM Tris pH 7.5, 1 mM magnesium chloride, 5% (w/v) glycerol, 5 mM DTT) and well solution (1.7 M ammonium sulfate, 100 mM sodium acetate pH 5.0, 200 mM magnesium chloride, 10% (w/v) glycerol), VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Nov 1, 2010 / Details: custom |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.797→29.705 Å / Num. all: 23542 / Num. obs: 18462 / % possible obs: 78.42 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 51.89 Å2 / Net I/σ(I): 2 |
Reflection shell | Resolution: 2.797→2.944 Å / Mean I/σ(I) obs: 2 / % possible all: 31 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2om2 Resolution: 2.797→29.705 Å / SU ML: 0.41 / σ(F): 0.71 / 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 / Bsol: 36.758 Å2 / ksol: 0.318 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.797→29.705 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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