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- PDB-6tju: X-ray structure of C-terminal domain of human T-cell lymphotropic... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6tju | ||||||
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Title | X-ray structure of C-terminal domain of human T-cell lymphotropic virus type 1 (HTLV-1) | ||||||
![]() | Pol protein | ||||||
![]() | TRANSFERASE / HTLV-1 / integrase / deltaretrovirus / DNA-binding | ||||||
Function / homology | ![]() DNA integration / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / DNA recombination / nucleic acid binding / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Barski, M. / Maertens, G.N. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of the deltaretroviral intasome in complex with the PP2A regulatory subunit B56γ. Authors: Michał S Barski / Jordan J Minnell / Zuzana Hodakova / Valerie E Pye / Andrea Nans / Peter Cherepanov / Goedele N Maertens / ![]() Abstract: Human T-cell lymphotropic virus type 1 (HTLV-1) is a deltaretrovirus and the most oncogenic pathogen. Many of the ~20 million HTLV-1 infected people will develop severe leukaemia or an ALS-like motor ...Human T-cell lymphotropic virus type 1 (HTLV-1) is a deltaretrovirus and the most oncogenic pathogen. Many of the ~20 million HTLV-1 infected people will develop severe leukaemia or an ALS-like motor disease, unless a therapy becomes available. A key step in the establishment of infection is the integration of viral genetic material into the host genome, catalysed by the retroviral integrase (IN) enzyme. Here, we use X-ray crystallography and single-particle cryo-electron microscopy to determine the structure of the functional deltaretroviral IN assembled on viral DNA ends and bound to the B56γ subunit of its human host factor, protein phosphatase 2 A. The structure reveals a tetrameric IN assembly bound to two molecules of the phosphatase via a conserved short linear motif. Insight into the deltaretroviral intasome and its interaction with the host will be crucial for understanding the pattern of integration events in infected individuals and therefore bears important clinical implications. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 55.9 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 423.6 KB | Display | ![]() |
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Full document | ![]() | 423.6 KB | Display | |
Data in XML | ![]() | 5 KB | Display | |
Data in CIF | ![]() | 6.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6qbtC ![]() 6qbvC ![]() 6qbwC ![]() 6toqC ![]() 7pelC ![]() 5lljS 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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Components on special symmetry positions |
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Components
#1: Protein | Mass: 7609.704 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.45 % / Description: rhombohedral |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: 1.2 M ammonium tartrate dibasic, 150 mM NaCl |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: May 10, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→39.77 Å / Num. obs: 41483 / % possible obs: 100 % / Redundancy: 5.4 % / CC1/2: 0.993 / Rmerge(I) obs: 0.077 / Rpim(I) all: 0.055 / Rrim(I) all: 0.095 / Χ2: 0.89 / Net I/σ(I): 7.4 |
Reflection shell | Resolution: 1.8→1.84 Å / Rmerge(I) obs: 0.711 / Mean I/σ(I) obs: 1.8 / Num. unique obs: 2513 / CC1/2: 0.354 / Rpim(I) all: 0.503 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5LLJ Resolution: 1.8→39.77 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.952 / SU B: 12.671 / SU ML: 0.144 / Cross valid method: FREE R-VALUE / ESU R: 0.133 / ESU R Free: 0.117 Details: Hydrogens have been added in their 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.44 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→39.77 Å
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Refine LS restraints |
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LS refinement shell |
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