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Yorodumi- PDB-7dop: Structural insights into viral RNA capping and plasma membrane ta... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7dop | |||||||||||||||||||||||||||||||||
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| Title | Structural insights into viral RNA capping and plasma membrane targeting by Chikungunya virus nonstructural protein 1 | |||||||||||||||||||||||||||||||||
Components | Nonstructural Protein 1 | |||||||||||||||||||||||||||||||||
Keywords | VIRAL PROTEIN / nonstructural protein / Chikungunya virus / RNA cap / replication / membrane associations | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationADP-ribose 1''-phosphate phosphatase / host cell filopodium / mRNA methyltransferase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide adenylyltransferase / polynucleotide 5'-phosphatase activity / poly(A) RNA polymerase activity / mRNA modification / regulation of cytoskeleton organization ...ADP-ribose 1''-phosphate phosphatase / host cell filopodium / mRNA methyltransferase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide adenylyltransferase / polynucleotide 5'-phosphatase activity / poly(A) RNA polymerase activity / mRNA modification / regulation of cytoskeleton organization / symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity / 7-methylguanosine mRNA capping / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / cysteine-type peptidase activity / Transferases; Transferring one-carbon groups; Methyltransferases / host cell cytoplasmic vesicle membrane / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / nucleoside-triphosphate phosphatase / methylation / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / symbiont-mediated suppression of host innate immune response / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated suppression of host gene expression / RNA-directed RNA polymerase / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / GTP binding / host cell nucleus / host cell plasma membrane / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / metal ion binding / membrane Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | Chikungunya virus strain S27-African prototype | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.38 Å | |||||||||||||||||||||||||||||||||
Authors | Zhang, K. / Law, Y.S. / Law, M.C.Y. / Tan, Y.B. / Wirawan, M. / Luo, D.H. | |||||||||||||||||||||||||||||||||
Citation | Journal: Cell Host Microbe / Year: 2021Title: Structural insights into viral RNA capping and plasma membrane targeting by Chikungunya virus nonstructural protein 1. Authors: Kuo Zhang / Yee-Song Law / Michelle Cheok Yien Law / Yaw Bia Tan / Melissa Wirawan / Dahai Luo / ![]() Abstract: Chikungunya virus (CHIKV) causes a debilitating arthralgic inflammatory disease in humans. The multifunctional CHIKV protein, nsP1, facilitates virus RNA replication and transcription by anchoring ...Chikungunya virus (CHIKV) causes a debilitating arthralgic inflammatory disease in humans. The multifunctional CHIKV protein, nsP1, facilitates virus RNA replication and transcription by anchoring the viral replication complex (RC) to plasma membrane vesicles and synthesizing the viral RNA 5' cap-0. Here, we report a cryo-EM structure of CHIKV nsP1 at 2.38 Å resolution. Twelve copies of nsP1 form a crown-shaped ring structure with a 7.5-nm-wide channel for mediating communication and exchange between the viral RC and the host cell. The catalytic site for viral RNA capping is located in a tunnel that is shaped by neighboring nsP1 molecules. Two membrane-association loops target nsP1 to the inner leaflet of the plasma membrane via palmitoylation and hydrophobic and electrostatic interactions. Our study provides the structural basis of viral RNA capping and RC assembly mediated by nsP1 and guides the development of antivirals targeting these essential steps of virus infection. | |||||||||||||||||||||||||||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7dop.cif.gz | 907.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7dop.ent.gz | 757.4 KB | Display | PDB format |
| PDBx/mmJSON format | 7dop.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7dop_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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| Full document | 7dop_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 7dop_validation.xml.gz | 125.7 KB | Display | |
| Data in CIF | 7dop_validation.cif.gz | 196.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/do/7dop ftp://data.pdbj.org/pub/pdb/validation_reports/do/7dop | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 30796MC M: map data used to model this data 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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Components
| #1: Protein | Mass: 62056.539 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chikungunya virus strain S27-African prototypeStrain: S27-African prototype / Production host: Homo sapiens (human) / References: UniProt: Q8JUX6#2: Chemical | ChemComp-ZN / Has ligand of interest | N | Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Nonstructural Protein 1 / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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| Source (natural) | Organism: Chikungunya virus strain S27-African prototype |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.8 |
| Specimen | Conc.: 0.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Cs: 2.7 mm |
| Image recording | Electron dose: 53 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.18.2_3874: / Classification: refinement | ||||||||||||||||||||||||
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| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.38 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 269498 / Symmetry type: POINT | ||||||||||||||||||||||||
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About Yorodumi



Chikungunya virus strain S27-African prototype
Citation
UCSF Chimera






PDBj


Homo sapiens (human)

