Cryo-EM model of virion-sized HEV virion-sized capsid
by single particle (icosahedral) reconstruction, at 10.5 A resolution

#1: Biological unit as complete icosahedral assembly, Made by Jmol
#2: Biological unit as icosahedral pentamer, Made by Jmol
#3: Biological unit as icosahedral 23 hexamer, Made by Jmol
#4: Depositted structure unit, Made by Jmol
#5: Superimposing with simplified surface model of EM map, EMDB-5173, Made by Jmol
#6: Superimposing with EM 3D map: EMDB-5173, Made by UCSF CHIMERA
#7: Superimposing with EM 3D map: EMDB-5173, Made by UCSF CHIMERA
Entry | |
| Summary | |
| Database / ID | PORTEIN DATA BANK (PDB) / 3iyo |
|---|---|
| Title | Cryo-EM model of virion-sized HEV virion-sized capsid |
| Descriptor | Capsid protein |
| Keywords | VIRUS, Amino Acid Sequence, Capsid, Capsid Proteins, Cryoelectron Microscopy, Dimerization, Image Processing, Computer-Assisted, Molecular Sequence Data, hepatitis E virus, Protein Conformation, Protein Folding, Protein Structure, Recombinant viral capsid, Virus Assembly, icosahedral virus |
| PDBj Mine pages | Summary, Structural Details, Experimental Details, Functional Details |
| Other databases | RCSB-PDB, PDBe, CATH, CE, FSSP, SCOP, VAST |
| Structure Visualization | |
| Movies | Movie Page#1: Biological unit as complete icosahedral assembly, Made by Jmol #2: Biological unit as icosahedral pentamer, Made by Jmol #3: Biological unit as icosahedral 23 hexamer, Made by Jmol #4: Depositted structure unit, Made by Jmol #5: Superimposing with simplified surface model of EM map, EMDB-5173, Made by Jmol #6: Superimposing with EM 3D map: EMDB-5173, Made by UCSF CHIMERA #7: Superimposing with EM 3D map: EMDB-5173, Made by UCSF CHIMERA |
| Structure viewers | Yorodumi, jV4, Jmol, Biological unit (Images, jV) |
| Related Structure Data | |
| Related Entries |
Fit: target map of fitting |
| Similar strucutres (beta) |
List of similar structure data about Omokage system |
Article | |
| Citation - primary | |
| Article | J.Biol.Chem., Vol. , Page: - , Year: 2010, |
|---|---|
| Title | Structural basis for the RNA-dependent assembly pathway of hepatitis E virion-sized particles |
| Authors | Xing, L., Mayazaki, N., Li, T.C., Simons, M.N., Wall, J.S., Moore, M., Wang, C.Y., Takeda, N., Wakita, T., Miyamura, T., Cheng, R.H. |
Components | |
| ID 1 : Capsid protein | |
| Image | ![]() ![]() |
|---|---|
| Description | Capsid protein |
| Type | polypeptide(L) |
| Formula weight | 71032.531 Da |
| Number of molecules | 3 |
| ID | 1 |
| Source | Method: Isolated from a natural source Common name: HEV NCBI taxonomy: ID:12461Organism scientific: Hepatitis E virus |
| Links | UniProt: Q1AHV0, Sequence view |
Sample | |
| Assembly | |
| Aggregation state | PARTICLE |
|---|---|
| Composition | 1 |
| Experimental Mass | 11.8 |
| Mass-estimation Method | STEM |
| Theoretical Mass | 12.2 |
| Name | Hepatitis E capsid |
| Num components | 2 |
| Entity assembly | |
| Assembly-ID | 1 |
| Name | hepatitis E virus |
| Type | VIRUS |
| Virus entity | |
| Empty | NO |
| Enveloped | NO |
| Ictvdb id | 00.084.0.01.001 |
| Virus host category | VERTEBRATES |
| Virus host species | Homo sapiens |
| Virus isolate | STRAIN |
| Virus type | VIRUS-LIKE PARTICLE |
| Buffer | |
| Name | MES-K buffer |
| Experiment | |
| Reconstruction method | SINGLE PARTICLE |
| Specimen type | VITREOUS ICE (CRYO EM) |
| Sample preparation | |
| Details | 20mM MES-K |
| pH | 6.2 |
| Sample concentration | 1 mg/ml |
| Vitrification | |
| Cryogen name | ETHANE |
| Instrument | manual plunger |
| Temp | 93 Kelvin |
| Experiment | |
| Method | ELECTRON MICROSCOPY |
Electron Microscopy | |
| Imaging | |
| Microscope | Model: OTHER |
|---|---|
| Electron gun | |
| Electron source | FIELD EMISSION GUN |
| Accelerating voltage | 200 kV |
| Electron dose | 10 e/A**2 |
| Illumination mode | FLOOD BEAM |
| Lens | |
| Mode | BRIGHT FIELD |
| Magnification | Nominal: 50000 X |
| Cs | Nominal: 2.0 mm |
| Detector distance | 0.0 |
| Specimen holder | |
| Specimen holder | Model: GATAN LIQUID NITROGEN, Type: single-tilt |
| Tilt angle | Min: 0.0 degrees, Max: 0.0 degrees |
| Detector | |
| Type | TVIPS TemCam-F415 |
Processing | |
| 2D projection selection | |
| Software name | Situs |
|---|---|
| Single particle entity | |
| Symmetry type | ICOSAHEDRAL |
| 3D reconstruction | |
| CTF correction method | each micrograph |
| Method | Polar Fourier Transform (PFT) |
| Number of particles | 4348 |
| Resolution | 10.5 A |
| Resolution method | FSC at 0.5 cut-off |
| Software | P3DR |
| 3D fitting | |
| Details | Monomer C were divided into Shell and Spike domains and separately fitted by manual docking using program O and followed by Situs |
| Refinement Protocol | Rigid Body |
| Refinement Space | REAL |
| Software name | Situs |
| Target criteria | cross-correlation |
| 3D fitting list | |
| 3D fitting id | 1 |
| Pdb chain id | A |
| PDB entry ID | 2ZZQ |
| Refine hist | |
| Cycle id | LAST |
| Refine id | ELECTRON MICROSCOPY |
| Total atoms | 1397 |
| Protein atoms | 1397 |