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Yorodumi- PDB-6tqp: Structural insight into tanapoxvirus mediated inhibition of apoptosis -
+Open data
-Basic information
Entry | Database: PDB / ID: 6tqp | |||||||||
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Title | Structural insight into tanapoxvirus mediated inhibition of apoptosis | |||||||||
Components |
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Keywords | APOPTOSIS / Pox virus / Bcl-2 | |||||||||
Function / homology | Function and homology information positive regulation of establishment of protein localization to mitochondrion / positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of growth / positive regulation of fibroblast apoptotic process / T cell apoptotic process / BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members / positive regulation of cysteine-type endopeptidase activity / positive regulation of thymocyte apoptotic process / fibroblast apoptotic process / execution phase of apoptosis ...positive regulation of establishment of protein localization to mitochondrion / positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of growth / positive regulation of fibroblast apoptotic process / T cell apoptotic process / BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members / positive regulation of cysteine-type endopeptidase activity / positive regulation of thymocyte apoptotic process / fibroblast apoptotic process / execution phase of apoptosis / Activation of PUMA and translocation to mitochondria / FOXO-mediated transcription of cell death genes / positive regulation of IRE1-mediated unfolded protein response / positive regulation of release of cytochrome c from mitochondria / TP53 Regulates Transcription of Genes Involved in Cytochrome C Release / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / positive regulation of intrinsic apoptotic signaling pathway / response to endoplasmic reticulum stress / intrinsic apoptotic signaling pathway / release of cytochrome c from mitochondria / cellular response to ionizing radiation / determination of adult lifespan / apoptotic signaling pathway / positive regulation of protein-containing complex assembly / activation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of neuron apoptotic process / cellular response to hypoxia / regulation of apoptotic process / mitochondrial outer membrane / DNA damage response / mitochondrion / membrane / cytosol Similarity search - Function | |||||||||
Biological species | Yaba-like disease virus Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8494094828 Å | |||||||||
Authors | Suraweera, C.D. / Hinds, M.G. / Kvansakul, M. | |||||||||
Funding support | Australia, 2items
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Citation | Journal: Febs J. / Year: 2020 Title: Structural insight into tanapoxvirus-mediated inhibition of apoptosis. Authors: Suraweera, C.D. / Anasir, M.I. / Chugh, S. / Javorsky, A. / Impey, R.E. / Hasan Zadeh, M. / Soares da Costa, T.P. / Hinds, M.G. / Kvansakul, M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6tqp.cif.gz | 138.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6tqp.ent.gz | 91.2 KB | Display | PDB format |
PDBx/mmJSON format | 6tqp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tq/6tqp ftp://data.pdbj.org/pub/pdb/validation_reports/tq/6tqp | HTTPS FTP |
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-Related 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: 17442.264 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Tanapox virus Bcl-2 homologe / Source: (gene. exp.) Yaba-like disease virus / Gene: 16L / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: Q9DHU6 |
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#2: Protein/peptide | Mass: 3210.520 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: PUMA BH3 motif (26-mer) / Source: (synth.) Homo sapiens (human) / References: UniProt: Q9BXH1 |
#3: Chemical | ChemComp-NA / |
#4: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.34 % / Description: long rod shape crystals with sharp edges |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 0.1 M Potassium thiocyanate, 30% PEG 2000MME |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Sep 28, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 1.849→32.45 Å / Num. obs: 15799 / % possible obs: 99.51 % / Redundancy: 5.5 % / Biso Wilson estimate: 36.7645901849 Å2 / CC1/2: 0.99 / Rmerge(I) obs: 0.066 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 1.85→1.89 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.072 / Num. unique obs: 15850 / CC1/2: 0.998 / % possible all: 99.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: previously solved structure of TNP_16L Resolution: 1.8494094828→32.4499523192 Å / SU ML: 0.297080171611 / Cross valid method: FREE R-VALUE / σ(F): 1.33787641762 / Phase error: 28.0186733218 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 54.7601363343 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8494094828→32.4499523192 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 36.5450173979 Å / Origin y: 30.7032327682 Å / Origin z: 18.4936300547 Å
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Refinement TLS group | Selection details: all |