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- PDB-6fln: Crystal structure of the human TRIM25 coiled-coil and PRYSPRY domains -
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Open data
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Basic information
Entry | Database: PDB / ID: 6fln | ||||||
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Title | Crystal structure of the human TRIM25 coiled-coil and PRYSPRY domains | ||||||
![]() | E3 ubiquitin/ISG15 ligase TRIM25 | ||||||
![]() | PROTEIN BINDING / Coiled-coil / PRYSPRY domain / TRIM proteins / E3 ligase | ||||||
Function / homology | ![]() : / RIG-I binding / regulation of viral entry into host cell / suppression of viral release by host / negative regulation of viral entry into host cell / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / response to vitamin D / TRAF6 mediated IRF7 activation / cytoplasmic pattern recognition receptor signaling pathway / RSV-host interactions ...: / RIG-I binding / regulation of viral entry into host cell / suppression of viral release by host / negative regulation of viral entry into host cell / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / response to vitamin D / TRAF6 mediated IRF7 activation / cytoplasmic pattern recognition receptor signaling pathway / RSV-host interactions / protein monoubiquitination / ligase activity / TRAF6 mediated NF-kB activation / antiviral innate immune response / viral release from host cell / protein K48-linked ubiquitination / ERAD pathway / cellular response to leukemia inhibitory factor / Negative regulators of DDX58/IFIH1 signaling / Termination of translesion DNA synthesis / RING-type E3 ubiquitin transferase / DDX58/IFIH1-mediated induction of interferon-alpha/beta / PKR-mediated signaling / Evasion by RSV of host interferon responses / ISG15 antiviral mechanism / positive regulation of DNA-binding transcription factor activity / cytoplasmic stress granule / response to estrogen / ubiquitin-protein transferase activity / SARS-CoV-1 activates/modulates innate immune responses / regulation of protein localization / Interferon gamma signaling / ubiquitin protein ligase activity / Ovarian tumor domain proteases / positive regulation of NF-kappaB transcription factor activity / TRAF3-dependent IRF activation pathway / ubiquitin-dependent protein catabolic process / positive regulation of canonical NF-kappaB signal transduction / response to oxidative stress / transcription coactivator activity / nuclear body / cadherin binding / innate immune response / SARS-CoV-2 activates/modulates innate and adaptive immune responses / RNA binding / nucleoplasm / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Cusack, S. / Lethier, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition. Authors: Koliopoulos, M.G. / Lethier, M. / van der Veen, A.G. / Haubrich, K. / Hennig, J. / Kowalinski, E. / Stevens, R.V. / Martin, S.R. / Reis E Sousa, C. / Cusack, S. / Rittinger, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 230.8 KB | Display | ![]() |
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PDB format | ![]() | 185.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449.7 KB | Display | ![]() |
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Full document | ![]() | 456.5 KB | Display | |
Data in XML | ![]() | 36.5 KB | Display | |
Data in CIF | ![]() | 49.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5nt1C ![]() 5nt2C ![]() 6flmSC ![]() 4ltbS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / Refine code: _
NCS ensembles :
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Components
#1: Protein | Mass: 50288.484 Da / Num. of mol.: 3 / Fragment: coiled-coil and PRYSPRY domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: Q14258, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases), RING-type E3 ubiquitin transferase |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.74 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: Protein at 10 mg/ml was mixed in 2:1 ratio with mother liquor containing 0.2 M sodium formate, 14% PEG 3350 and 0.1 M bis-Tris pH 6.5. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Nov 16, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.072 Å / Relative weight: 1 |
Reflection | Resolution: 3.6→137.85 Å / Num. obs: 24552 / % possible obs: 99.5 % / Redundancy: 5.36 % / CC1/2: 0.999 / Rmerge(I) obs: 0.136 / Rrim(I) all: 0.151 / Net I/σ(I): 8.18 |
Reflection shell | Resolution: 3.6→3.69 Å / Redundancy: 5.51 % / Rmerge(I) obs: 2.38 / CC1/2: 0.569 / Rrim(I) all: 2.64 / Χ2: 0.75 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: Separate coiled-coil (PDB:4LTB) and PRYSPRY (PDB:6FLM) domains Resolution: 3.6→137.85 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.921 / SU B: 75.375 / SU ML: 0.929 / Cross valid method: THROUGHOUT / ESU R Free: 0.722 / 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: 219.61 Å2
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Refinement step | Cycle: 1 / Resolution: 3.6→137.85 Å
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Refine LS restraints |
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