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Yorodumi- PDB-5tl7: Crystal structure of SARS-CoV papain-like protease in complex wit... -
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-Basic information
Entry | Database: PDB / ID: 5tl7 | |||||||||
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Title | Crystal structure of SARS-CoV papain-like protease in complex with C-terminal domain mouse ISG15 | |||||||||
Components |
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Keywords | Signaling protein/Hydrolase / Signaling protein / Hydrolase / Signaling protein-Hydrolase complex | |||||||||
Function / homology | Function and homology information positive regulation of protein oligomerization / Termination of translesion DNA synthesis / ISG15 antiviral mechanism / ISG15-protein conjugation / PKR-mediated signaling / regulation of type II interferon production / Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / Transcription of SARS-CoV-1 sgRNAs / protein localization to mitochondrion ...positive regulation of protein oligomerization / Termination of translesion DNA synthesis / ISG15 antiviral mechanism / ISG15-protein conjugation / PKR-mediated signaling / regulation of type II interferon production / Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / Transcription of SARS-CoV-1 sgRNAs / protein localization to mitochondrion / response to type I interferon / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-1 genome / K48-linked deubiquitinase activity / host cell endoplasmic reticulum / negative regulation of type I interferon-mediated signaling pathway / K63-linked deubiquitinase activity / negative regulation of viral genome replication / SARS-CoV-1 modulates host translation machinery / viral transcription / positive regulation of interleukin-10 production / positive regulation of bone mineralization / negative regulation of protein ubiquitination / Transferases; Transferring one-carbon groups; Methyltransferases / positive regulation of interferon-beta production / positive regulation of erythrocyte differentiation / integrin-mediated signaling pathway / response to bacterium / response to virus / modification-dependent protein catabolic process / protein tag activity / SARS-CoV-1 activates/modulates innate immune responses / positive regulation of type II interferon production / integrin binding / 5'-3' RNA helicase activity / Lyases; Phosphorus-oxygen lyases / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / : / double membrane vesicle viral factory outer membrane / SARS coronavirus main proteinase / host cell endosome / 3'-5'-RNA exonuclease activity / host cell endoplasmic reticulum-Golgi intermediate compartment / symbiont-mediated degradation of host mRNA / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / omega peptidase activity / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / host cell Golgi apparatus / symbiont-mediated perturbation of host ubiquitin-like protein modification / defense response to virus / mRNA (nucleoside-2'-O-)-methyltransferase activity / endonuclease activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / DNA helicase / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / single-stranded RNA binding / host cell perinuclear region of cytoplasm / viral protein processing / lyase activity / RNA helicase / defense response to bacterium / 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 / innate immune response / DNA-templated transcription / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / ubiquitin protein ligase binding / ATP hydrolysis activity / proteolysis / zinc ion binding / extracellular region / ATP binding / membrane / identical protein binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) SARS coronavirus | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.44 Å | |||||||||
Authors | Daczkowski, C.D. / Dzimianski, J.V. / Pegan, S.D. | |||||||||
Funding support | United States, 2items
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Citation | Journal: J. Mol. Biol. / Year: 2017 Title: Structural Insights into the Interaction of Coronavirus Papain-Like Proteases and Interferon-Stimulated Gene Product 15 from Different Species. Authors: Daczkowski, C.M. / Dzimianski, J.V. / Clasman, J.R. / Goodwin, O. / Mesecar, A.D. / Pegan, S.D. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5tl7.cif.gz | 328.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5tl7.ent.gz | 269.9 KB | Display | PDB format |
PDBx/mmJSON format | 5tl7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tl/5tl7 ftp://data.pdbj.org/pub/pdb/validation_reports/tl/5tl7 | HTTPS FTP |
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-Related structure data
Related structure data | 5tl6C 5tlaC 3e9sS 5jzeS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 9280.692 Da / Num. of mol.: 2 / Fragment: C-terminal domain (UNP residues 78-155 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Isg15, G1p2, Ucrp / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q64339 #2: Protein | Mass: 35809.629 Da / Num. of mol.: 2 / Fragment: UNP residues 1541-1855 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SARS coronavirus / Gene: rep, 1a-1b / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P0C6X7, ubiquitinyl hydrolase 1, SARS coronavirus main proteinase, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases, RNA-directed RNA polymerase, DNA ...References: UniProt: P0C6X7, ubiquitinyl hydrolase 1, SARS coronavirus main proteinase, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases, RNA-directed RNA polymerase, DNA helicase, RNA helicase, Transferases; Transferring one-carbon groups; Methyltransferases, Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters, Hydrolases; Acting on ester bonds #3: Chemical | #4: Water | ChemComp-HOH / | |
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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: 2.21 Å3/Da / Density % sol: 44.23 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 65% (v/v) MPD, 0.1 M Tris [pH 8.0], supplemented with 30% (w/v) Trimethylamine N-oxide dihydrate additive in a 1:5 dilution |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.9786 Å |
Detector | Type: RAYONIX MX-300 / Detector: CCD / Date: Jun 26, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9786 Å / Relative weight: 1 |
Reflection | Resolution: 2.44→72.23 Å / Num. obs: 29922 / % possible obs: 99.1 % / Redundancy: 2.4 % / Rmerge(I) obs: 0.099 / Net I/σ(I): 18 |
Reflection shell | Resolution: 2.44→2.53 Å / Rmerge(I) obs: 0.742 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3E9S,5JZE Resolution: 2.44→72.23 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.905 / SU B: 24.002 / SU ML: 0.264 / Cross valid method: THROUGHOUT / ESU R: 0.697 / ESU R Free: 0.315 / 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: 64.266 Å2
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Refinement step | Cycle: 1 / Resolution: 2.44→72.23 Å
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