[English] 日本語
Yorodumi- PDB-8f2q: Human Parvovirus B19 Nonstructural NS1 Protein NLS bound to Impor... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8f2q | ||||||
---|---|---|---|---|---|---|---|
Title | Human Parvovirus B19 Nonstructural NS1 Protein NLS bound to Importin Alpha 2 | ||||||
Components |
| ||||||
Keywords | TRANSPORT PROTEIN / Importin / nuclear / transport / nls | ||||||
Function / homology | Function and homology information rolling hairpin viral DNA replication / symbiont-mediated arrest of host cell cycle during G2/M transition / symbiont-mediated perturbation of host transcription / Sensing of DNA Double Strand Breaks / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters / nuclear import signal receptor activity ...rolling hairpin viral DNA replication / symbiont-mediated arrest of host cell cycle during G2/M transition / symbiont-mediated perturbation of host transcription / Sensing of DNA Double Strand Breaks / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters / nuclear import signal receptor activity / helicase activity / symbiont-mediated activation of host apoptosis / protein import into nucleus / cytoplasmic stress granule / host cell / DNA helicase / endonuclease activity / DNA-binding transcription factor binding / DNA replication / postsynaptic density / host cell nucleus / glutamatergic synapse / ATP hydrolysis activity / DNA binding / nucleoplasm / ATP binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Human parvovirus B19 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Cross, E.M. / Forwood, J.K. | ||||||
Funding support | 1items
| ||||||
Citation | Journal: Antiviral Res. / Year: 2023 Title: Importin alpha / beta-dependent nuclear transport of human parvovirus B19 nonstructural protein 1 is essential for viral replication. Authors: Alvisi, G. / Manaresi, E. / Cross, E.M. / Hoad, M. / Akbari, N. / Pavan, S. / Ariawan, D. / Bua, G. / Petersen, G.F. / Forwood, J. / Gallinella, G. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 8f2q.cif.gz | 209.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb8f2q.ent.gz | 134.7 KB | Display | PDB format |
PDBx/mmJSON format | 8f2q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8f2q_validation.pdf.gz | 443.8 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 8f2q_full_validation.pdf.gz | 446.4 KB | Display | |
Data in XML | 8f2q_validation.xml.gz | 16 KB | Display | |
Data in CIF | 8f2q_validation.cif.gz | 21.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f2/8f2q ftp://data.pdbj.org/pub/pdb/validation_reports/f2/8f2q | HTTPS FTP |
-Related structure data
Related structure data | 4uafS S: Starting model for refinement |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 55268.473 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kpna2, Rch1 / Production host: Escherichia coli (E. coli) / References: UniProt: P52293 |
---|---|
#2: Protein/peptide | Mass: 1185.442 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Human parvovirus B19 References: UniProt: Q9PZT1, Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters, DNA helicase |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.07 Å3/Da / Density % sol: 59.99 % |
---|---|
Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: 0.7M sodium citrate, 0.1M HEPES pH6.5, 0.01M DTT |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.95373 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 15, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95373 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→29.54 Å / Num. obs: 20091 / % possible obs: 99.8 % / Redundancy: 3.8 % / Biso Wilson estimate: 45.78 Å2 / CC1/2: 0.947 / Rmerge(I) obs: 0.16 / Net I/σ(I): 6.3 |
Reflection shell | Resolution: 2.7→2.83 Å / Rmerge(I) obs: 1.045 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 2620 / CC1/2: 0.563 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4uaf Resolution: 2.7→29.54 Å / SU ML: 0.3467 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.1262 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
| |||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 53.62 Å2 | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→29.54 Å
| |||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||
LS refinement shell |
|