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Yorodumi- PDB-3ab3: Crystal structure of p115RhoGEF RGS domain in complex with G alpha 13 -
+Open data
-Basic information
Entry | Database: PDB / ID: 3ab3 | ||||||
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Title | Crystal structure of p115RhoGEF RGS domain in complex with G alpha 13 | ||||||
Components |
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Keywords | SIGNALING PROTEIN/MEMBRANE PROTEIN / SIGNAL TRANSDUCTION / PROTEIN COMPLEX / GTP-BINDING / MEMBRANE / TRANSDUCER / Lipoprotein / Nucleotide-binding / Palmitate / Phosphoprotein / GTPase activation / Guanine-nucleotide releasing factor / SIGNALING PROTEIN-MEMBRANE PROTEIN complex | ||||||
Function / homology | Function and homology information D5 dopamine receptor binding / PLC beta mediated events / Adenylate cyclase inhibitory pathway / zymogen granule / CDC42 GTPase cycle / regulation of fibroblast migration / ADP signalling through P2Y purinoceptor 12 / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Thromboxane signalling through TP receptor / NRAGE signals death through JNK ...D5 dopamine receptor binding / PLC beta mediated events / Adenylate cyclase inhibitory pathway / zymogen granule / CDC42 GTPase cycle / regulation of fibroblast migration / ADP signalling through P2Y purinoceptor 12 / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Thromboxane signalling through TP receptor / NRAGE signals death through JNK / RAC1 GTPase cycle / Thrombin signalling through proteinase activated receptors (PARs) / G-protein activation / Extra-nuclear estrogen signaling / G alpha (12/13) signalling events / positive regulation of NAD(P)H oxidase activity / vesicle fusion / G alpha (i) signalling events / negative regulation of vascular associated smooth muscle cell migration / GTP metabolic process / GTPase activating protein binding / regulation of small GTPase mediated signal transduction / dopamine receptor signaling pathway / branching involved in blood vessel morphogenesis / RHOB GTPase cycle / NRAGE signals death through JNK / RHOC GTPase cycle / negative regulation of vascular associated smooth muscle cell proliferation / positive regulation of macroautophagy / negative regulation of apoptotic signaling pathway / Rho protein signal transduction / RHOA GTPase cycle / G protein-coupled serotonin receptor binding / positive regulation of vascular associated smooth muscle cell proliferation / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / GTPase activator activity / guanyl-nucleotide exchange factor activity / positive regulation of superoxide anion generation / G protein-coupled receptor binding / brush border membrane / brain development / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / platelet activation / regulation of blood pressure / GDP binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / melanosome / midbody / positive regulation of cytosolic calcium ion concentration / regulation of cell shape / angiogenesis / in utero embryonic development / cell differentiation / intracellular signal transduction / cell cycle / membrane raft / G protein-coupled receptor signaling pathway / cell division / protein domain specific binding / Golgi membrane / GTPase activity / centrosome / GTP binding / endoplasmic reticulum membrane / Golgi apparatus / RNA binding / membrane / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Kukimoto-Niino, M. / Mishima, C. / Shirouzu, M. / Kozasa, T. / Yokoyama, S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: Identification of critical residues in G(alpha)13 for stimulation of p115RhoGEF activity and the structure of the G(alpha)13-p115RhoGEF regulator of G protein signaling homology (RH) domain complex. Authors: Hajicek, N. / Kukimoto-Niino, M. / Mishima-Tsumagari, C. / Chow, C.R. / Shirouzu, M. / Terada, T. / Patel, M. / Yokoyama, S. / Kozasa, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ab3.cif.gz | 219.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ab3.ent.gz | 171.5 KB | Display | PDB format |
PDBx/mmJSON format | 3ab3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/3ab3 ftp://data.pdbj.org/pub/pdb/validation_reports/ab/3ab3 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-Protein , 2 types, 4 molecules ACBD
#1: Protein | Mass: 42363.418 Da / Num. of mol.: 2 Fragment: UNP RESIDUES 1-28 (G ALPHA I), UNP RESIDUES 47-377 (G ALPHA 13) Source method: isolated from a genetically manipulated source Details: ONE FUSED PROTEIN IS MADE OF RESIDUES 1-28 OF G ALPHA I, LINKER, AND RESIDUES 47-377 OF G ALPHA 13 Source: (gene. exp.) Mus musculus (house mouse) / Gene: Gna13, Gna-13 / Plasmid: PE060908-01 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 / References: UniProt: Q9DC51, UniProt: P27601 #2: Protein | Mass: 27648.441 Da / Num. of mol.: 2 / Fragment: N-TERMINAL RGS HOMOLOGY DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ARHGEF1 / Plasmid: PE080111-02 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 / References: UniProt: Q92888 |
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-Non-polymers , 4 types, 93 molecules
#3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Details
Sequence details | THE CHAINS A AND C INCLUDE N-TERMINAL RESIDUES 1-28 OF G ALPHA I, LINKER (ARG-SER-ALA) AND RESIDUES ...THE CHAINS A AND C INCLUDE N-TERMINAL RESIDUES 1-28 OF G ALPHA I, LINKER (ARG-SER-ALA) AND RESIDUES 47-377 OF G ALPHA 13 |
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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: 2.16 Å3/Da / Density % sol: 42.93 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 15% PEG 4000, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 21, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. obs: 37777 / % possible obs: 81.8 % / Observed criterion σ(I): -3 / Redundancy: 1.7 % / Biso Wilson estimate: 37.1 Å2 / Rsym value: 0.074 / Net I/σ(I): 9 |
Reflection shell | Resolution: 2.4→2.49 Å / Mean I/σ(I) obs: 2.3 / Rsym value: 0.296 / % possible all: 82.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1IAP, 1ZBC Resolution: 2.4→48.88 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 1175586.46 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 44.8937 Å2 / ksol: 0.360413 e/Å3 | ||||||||||||||||||||
Displacement parameters | Biso mean: 51.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→48.88 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.55 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Xplor file |
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