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Open data
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Basic information
| Entry | Database: PDB / ID: 6m16 | |||||||||
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| Title | Cryo-EM structures of SADS-CoV spike glycoproteins | |||||||||
Components | Spike glycoprotein | |||||||||
Keywords | VIRAL PROTEIN | |||||||||
| Function / homology | Function and homology informationhost cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated virion attachment to host cell / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion membrane / membrane Similarity search - Function | |||||||||
| Biological species | Swine acute diarrhea syndrome coronavirus | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.83 Å | |||||||||
Authors | Wang, X. / Yu, J. / Qiao, S. / Guo, R. | |||||||||
Citation | Journal: Nat Commun / Year: 2020Title: Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution. Authors: Jinfang Yu / Shuyuan Qiao / Runyu Guo / Xinquan Wang / ![]() Abstract: Porcine coronavirus SADS-CoV has been identified from suckling piglets with severe diarrhea in southern China in 2017. The SADS-CoV genome shares ~95% identity to that of bat α-coronavirus HKU2, ...Porcine coronavirus SADS-CoV has been identified from suckling piglets with severe diarrhea in southern China in 2017. The SADS-CoV genome shares ~95% identity to that of bat α-coronavirus HKU2, suggesting that SADS-CoV may have emerged from a natural reservoir in bats. Here we report the cryo-EM structures of HKU2 and SADS-CoV spike (S) glycoprotein trimers at 2.38 Å and 2.83 Å resolution, respectively. We systematically compare the domains of HKU2 spike with those of α-, β-, γ-, and δ-coronavirus spikes, showing that the S1 subunit N- and C-terminal domains of HKU2/SADS-CoV are ancestral domains in the evolution of coronavirus spike proteins. The connecting region after the fusion peptide in the S2 subunit of HKU2/SADS-CoV adopts a unique conformation. These results structurally demonstrate a close evolutionary relationship between HKU2/SADS-CoV and β-coronavirus spikes and provide insights into the evolution and cross-species transmission of coronaviruses. | |||||||||
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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 | 6m16.cif.gz | 526.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6m16.ent.gz | 431.3 KB | Display | PDB format |
| PDBx/mmJSON format | 6m16.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6m16_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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| Full document | 6m16_full_validation.pdf.gz | 1.5 MB | Display | |
| Data in XML | 6m16_validation.xml.gz | 76.9 KB | Display | |
| Data in CIF | 6m16_validation.cif.gz | 117.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m1/6m16 ftp://data.pdbj.org/pub/pdb/validation_reports/m1/6m16 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 30038MC ![]() 6m15C 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: 124780.586 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Swine acute diarrhea syndrome coronavirusProduction host: Trichoplusia ni (cabbage looper) / References: UniProt: A0A2P1G1L3#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Sugar | ChemComp-NAG / Has ligand of interest | N | Has protein modification | Y | Sequence details | The L1069-G1112 is expression tag for trimerization and W1113-K1120 is strep tag used for purification. | |
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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: SADS-CoV glycoprotein / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Swine acute diarrhea syndrome coronavirus |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| Buffer solution | pH: 7.2 |
| Specimen | Conc.: 0.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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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 |
| Image recording | Electron dose: 49.784 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| CTF correction | Type: NONE |
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| 3D reconstruction | Resolution: 2.83 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 152334 / Symmetry type: POINT |
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Swine acute diarrhea syndrome coronavirus
Citation
UCSF Chimera










PDBj
Trichoplusia ni (cabbage looper)

