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Yorodumi- PDB-4rqp: Crystal structure of the natually occurring empty particle of a c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4rqp | ||||||
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Title | Crystal structure of the natually occurring empty particle of a clinical C4 strain EV71 | ||||||
Components |
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Keywords | VIRUS / beta barrel / icosahedral virus / natually occurring empty particle with unknown function / replicate in host cell cytoplasm | ||||||
Function / homology | Function and homology information symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : ...symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | Enterovirus A71 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.151 Å | ||||||
Authors | Chen, R. / Lyu, K. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2015 Title: Crystal structures of enterovirus 71 (EV71) recombinant virus particles provide insights into vaccine design. Authors: Lyu, K. / Wang, G.C. / He, Y.L. / Han, J.F. / Ye, Q. / Qin, C.F. / Chen, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4rqp.cif.gz | 655.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4rqp.ent.gz | 539.5 KB | Display | PDB format |
PDBx/mmJSON format | 4rqp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rq/4rqp ftp://data.pdbj.org/pub/pdb/validation_reports/rq/4rqp | 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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Details | The biological assembly is a 60mer generated from the pentamer in the asymmetric unit by the following 12 operations: (x,y,z),(-x,-y,z),(-x,y,-z),(x,-y,-z),(y,z,x),(-y,-z,x),(-y,z,-x),(y,-z,-x),(z,x,y),(-z,-x,y),(-z,x,-y) and (z,-x,-y). The pentamer in the asymmetric unit is generated from the deposited PDB by the following transformations(r11,r12,r13,r21,r22,r23,r31,r32,r33,tx,tx,tz):(1,0,0,0,1,0,0,0,1,0,0,0), (0.3034, -0.8159, 0.4922, 0.808, 0.4941, 0.3209,-0.505, 0.3004, 0.8092, 1.689, -1.178, 0.6762), (-0.8062, 0.491, -0.3302, -0.5139, -0.3045, 0.802, 0.2932, 0.8162, 0.4978, 3.567, 0.5881, -0.3295), (-0.8135, -0.5065, 0.2856, 0.4827, -0.3143, 0.8174, -0.3243, 0.8029, 0.5002, 3.719, -0.6645, 0.4134) and (0.3089, 0.8069, -0.5034, -0.8107, 0.5002, 0.3043, 0.4974, 0.3141, 0.8087, 0.6959, 0.5791, -0.5132) |
-Components
#1: Protein | Mass: 32699.773 Da / Num. of mol.: 5 / Mutation: K550Q / Source method: isolated from a natural source / Source: (natural) Enterovirus A71 / Strain: a clinical C4 strain / References: UniProt: F6KTB0 #2: Protein | Mass: 26440.148 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Enterovirus A71 / Strain: a clinical C4 strain / References: UniProt: F6KTB0 #3: Protein | Mass: 35209.219 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Enterovirus A71 / Strain: a clinical C4 strain / References: UniProt: F6KTB0 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.88 Å3/Da / Density % sol: 68.33 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1M Imidazole,1.0M sodium acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.97916 Å |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Oct 2, 2010 |
Radiation | Monochromator: SI 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97916 Å / Relative weight: 1 |
Reflection | Resolution: 3.151→49.918 Å / Num. all: 209079 / Num. obs: 190018 / % possible obs: 90.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 3.15→3.2 Å / Rmerge(I) obs: 0.904 / % possible all: 89.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.151→49.918 Å / σ(F): 1.34 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3.151→49.918 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.1511→3.2298 Å
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