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Open data
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Basic information
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| Title | Local refinement of single HCoV-229E S protein | ||||||||||||||||||||||||||||||
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Keywords | human coronavirus 229E / spike protein / human aminopeptidase N / VIRAL PROTEIN | ||||||||||||||||||||||||||||||
| Biological species | Human coronavirus 229E | ||||||||||||||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.39 Å | ||||||||||||||||||||||||||||||
Authors | Hsu STD / Tsai YX | ||||||||||||||||||||||||||||||
| Funding support | Taiwan, 9 items
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Citation | Journal: Nat Commun / Year: 2025Title: Molecular basis of host recognition of human coronavirus 229E. Authors: Yu-Xi Tsai / Yu-Chun Chien / Min-Feng Hsu / Kay-Hooi Khoo / Shang-Te Danny Hsu / ![]() Abstract: Human coronavirus 229E (HCoV-229E) is the earliest CoV found to infect humans. It binds to the human aminopeptidase N (hAPN) through the receptor binding domain (RBD) of its spike (S) protein to ...Human coronavirus 229E (HCoV-229E) is the earliest CoV found to infect humans. It binds to the human aminopeptidase N (hAPN) through the receptor binding domain (RBD) of its spike (S) protein to achieve host recognition. We present the cryo-electron microscopy structure of two HCoV-229E S protein in complex with a dimeric hAPN to provide structural insights on how the HCoV-229E S protein opens up its RBD to engage with its host receptor, information that is currently missing among alphacoronaviruses to which HCoV-229E belong. We quantitatively profile the glycosylation of HCoV-229E S protein and hAPN to deduce the glyco-shielding effects pertinent to antigenicity and host recognition. Finally, we present an atomic model of fully glycosylated HCoV-229E S in complex with hAPN anchored on their respective membrane bilayers to recapitulate the structural basis of the first step of host infection by HCoV-229E. | ||||||||||||||||||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_38820.map.gz | 777 MB | EMDB map data format | |
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| Header (meta data) | emd-38820-v30.xml emd-38820.xml | 15.6 KB 15.6 KB | Display Display | EMDB header |
| Images | emd_38820.png | 52.3 KB | ||
| Filedesc metadata | emd-38820.cif.gz | 4.1 KB | ||
| Others | emd_38820_half_map_1.map.gz emd_38820_half_map_2.map.gz | 764.1 MB 764 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-38820 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-38820 | HTTPS FTP |
-Validation report
| Summary document | emd_38820_validation.pdf.gz | 1004.6 KB | Display | EMDB validaton report |
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| Full document | emd_38820_full_validation.pdf.gz | 1004.1 KB | Display | |
| Data in XML | emd_38820_validation.xml.gz | 21.2 KB | Display | |
| Data in CIF | emd_38820_validation.cif.gz | 25.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-38820 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-38820 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_38820.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.476 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_38820_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_38820_half_map_2.map | ||||||||||||
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Sample components
-Entire : Local refinement of single HCoV-229E S protein
| Entire | Name: Local refinement of single HCoV-229E S protein |
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| Components |
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-Supramolecule #1: Local refinement of single HCoV-229E S protein
| Supramolecule | Name: Local refinement of single HCoV-229E S protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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| Source (natural) | Organism: Human coronavirus 229E |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.6 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.39 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 253164 |
| Initial angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.1.1) |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.1.1) |
Movie
Controller
About Yorodumi




Keywords
Human coronavirus 229E
Authors
Taiwan, 9 items
Citation








Z (Sec.)
Y (Row.)
X (Col.)




































FIELD EMISSION GUN

