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Yorodumi- PDB-5awm: The Crystal Structure of JNK from Drosophila melanogaster Reveals... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5awm | |||||||||
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Title | The Crystal Structure of JNK from Drosophila melanogaster Reveals an Evolutionarily Conserved Topology with that of Mammalian JNK Proteins. | |||||||||
Components | Stress-activated protein kinase JNK | |||||||||
Keywords | TRANSFERASE / c-Jun N-terminal kinase / MAP kinase / Drosophila JNK pathway | |||||||||
Function / homology | Function and homology information collateral sprouting of injured axon / Formation of the cytosolic BSK 'scaffolding complex' / Formation of the nuclear AP-1 transcription factor 'scaffolding complex' / Transcriptional activtion by AP-1 transcription factor / Imd pathway / Activation of the AP-1 family of transcription factors / Interleukin-38 signaling / NRAGE signals death through JNK / chorion micropyle formation / embryonic anterior midgut (ectodermal) morphogenesis ...collateral sprouting of injured axon / Formation of the cytosolic BSK 'scaffolding complex' / Formation of the nuclear AP-1 transcription factor 'scaffolding complex' / Transcriptional activtion by AP-1 transcription factor / Imd pathway / Activation of the AP-1 family of transcription factors / Interleukin-38 signaling / NRAGE signals death through JNK / chorion micropyle formation / embryonic anterior midgut (ectodermal) morphogenesis / dorsal closure, spreading of leading edge cells / peptidoglycan recognition protein signaling pathway / imaginal disc fusion, thorax closure / imaginal disc-derived male genitalia morphogenesis / determination of digestive tract left/right asymmetry / FCERI mediated MAPK activation / Oxidative Stress Induced Senescence / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / melanization defense response / positive regulation of neuron remodeling / dorsal closure / mushroom body development / follicle cell of egg chamber development / JUN phosphorylation / dorsal appendage formation / positive regulation of border follicle cell migration / JUN kinase activity / engulfment of apoptotic cell / cellular response to arsenic-containing substance / axon extension / wound healing, spreading of epidermal cells / neuron development / long-term memory / MAP kinase activity / mitogen-activated protein kinase / vascular endothelial growth factor receptor signaling pathway / positive regulation of autophagy / JNK cascade / cellular response to cadmium ion / tumor necrosis factor-mediated signaling pathway / neuron projection morphogenesis / axon guidance / wound healing / cellular response to reactive oxygen species / cellular response to oxidative stress / antibacterial humoral response / response to heat / regulation of gene expression / response to oxidative stress / protein kinase activity / intracellular signal transduction / axon / protein serine/threonine kinase activity / dendrite / positive regulation of gene expression / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Drosophila melanogaster (fruit fly) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.79 Å | |||||||||
Authors | Boonserm, P. | |||||||||
Funding support | Thailand, 1items
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Citation | Journal: Bmc Struct.Biol. / Year: 2015 Title: The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteins. Authors: Chimnaronk, S. / Sitthiroongruang, J. / Srisucharitpanit, K. / Srisaisup, M. / Ketterman, A.J. / Boonserm, P. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5awm.cif.gz | 92 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5awm.ent.gz | 66.1 KB | Display | PDB format |
PDBx/mmJSON format | 5awm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aw/5awm ftp://data.pdbj.org/pub/pdb/validation_reports/aw/5awm | HTTPS FTP |
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-Related structure data
Related structure data | 2xs0S 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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Unit cell |
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-Components
#1: Protein | Mass: 45509.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: bsk, JNK, CG5680 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3)pLysS References: UniProt: P92208, mitogen-activated protein kinase | ||
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#2: Chemical | ChemComp-ANP / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.23 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 25% (w/v) PEG 4000, 0.1 M Tris-HCl pH 8.5 and 0.2 M MgCl2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL32XU / Wavelength: 1 Å |
Detector | Type: RAYONIX MX225HE / Detector: CCD / Date: Jan 28, 2012 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.58→28.28 Å / Num. obs: 51133 / % possible obs: 99.4 % / Redundancy: 4.3 % / Biso Wilson estimate: 20.3 Å2 / Rmerge(I) obs: 0.062 / Net I/av σ(I): 11.8 / Net I/σ(I): 0.118 |
Reflection shell | Resolution: 1.58→1.66 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.794 / Mean I/σ(I) obs: 1.8 / % possible all: 97.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2XS0 Resolution: 1.79→28.28 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.935 / SU B: 2.468 / SU ML: 0.078 / Cross valid method: THROUGHOUT / ESU R: 0.126 / ESU R Free: 0.125 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.457 Å2
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Refinement step | Cycle: LAST / Resolution: 1.79→28.28 Å
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