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Yorodumi- EMDB-39396: Localized reconstruction of Hepatitis B virus surface antigen dim... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-39396 | ||||||||||||||||||||||||
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Title | Localized reconstruction of Hepatitis B virus surface antigen dimer in the subviral particle with D2 symmetry from dataset A0 | ||||||||||||||||||||||||
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Sample |
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Keywords | Surface antigen / Localized reconstruction / VIRAL PROTEIN | ||||||||||||||||||||||||
Function / homology | Large envelope protein S / Major surface antigen from hepadnavirus / caveolin-mediated endocytosis of virus by host cell / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / virion membrane / membrane / Large envelope protein Function and homology information | ||||||||||||||||||||||||
Biological species | Hepatitis B virus ayw/China/Tibet127/2002 | ||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||||||||||||||||||||
Authors | Wang T / Cao L / Mu A / Wang Q / Rao ZH | ||||||||||||||||||||||||
Funding support | China, 7 items
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Citation | Journal: Science / Year: 2024 Title: Inherent symmetry and flexibility in hepatitis B virus subviral particles. Authors: Quan Wang / Tao Wang / Lin Cao / An Mu / Sheng Fu / Peipei Wang / Yan Gao / Wenxin Ji / Zhenyu Liu / Zhanqiang Du / Luke W Guddat / Wenchi Zhang / Shuang Li / Xuemei Li / Zhiyong Lou / ...Authors: Quan Wang / Tao Wang / Lin Cao / An Mu / Sheng Fu / Peipei Wang / Yan Gao / Wenxin Ji / Zhenyu Liu / Zhanqiang Du / Luke W Guddat / Wenchi Zhang / Shuang Li / Xuemei Li / Zhiyong Lou / Xiangxi Wang / Zhongyu Hu / Zihe Rao / Abstract: Chronic hepatitis B virus (HBV) infection poses a major global health challenge with massive morbidity and mortality. Despite a preventive vaccine, current treatments provide limited virus clearance, ...Chronic hepatitis B virus (HBV) infection poses a major global health challenge with massive morbidity and mortality. Despite a preventive vaccine, current treatments provide limited virus clearance, necessitating lifelong commitment. The HBV surface antigen (HBsAg) is crucial for diagnosis and prognosis, yet its high-resolution structure and assembly on the virus envelope remain elusive. Utilizing extensive datasets and advanced cryo-electron microscopy analysis, we present structural insights into HBsAg at a near-atomic resolution of 3.7 angstroms. HBsAg homodimers assemble into subviral particles with - and -like quasisymmetry, elucidating the dense-packing rules and structural adaptability of HBsAg. These findings provide insights into how HBsAg assembles into higher-order filaments and interacts with the capsid to form virions. | ||||||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_39396.map.gz | 84.9 MB | EMDB map data format | |
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Header (meta data) | emd-39396-v30.xml emd-39396.xml | 21.8 KB 21.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_39396_fsc.xml | 10.8 KB | Display | FSC data file |
Images | emd_39396.png | 50.5 KB | ||
Masks | emd_39396_msk_1.map | 91.1 MB | Mask map | |
Filedesc metadata | emd-39396.cif.gz | 6.4 KB | ||
Others | emd_39396_additional_1.map.gz emd_39396_half_map_1.map.gz emd_39396_half_map_2.map.gz | 20.8 MB 82.2 MB 82.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-39396 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-39396 | HTTPS FTP |
-Validation report
Summary document | emd_39396_validation.pdf.gz | 658.4 KB | Display | EMDB validaton report |
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Full document | emd_39396_full_validation.pdf.gz | 658 KB | Display | |
Data in XML | emd_39396_validation.xml.gz | 17.9 KB | Display | |
Data in CIF | emd_39396_validation.cif.gz | 23.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39396 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39396 | HTTPS FTP |
-Related structure data
Related structure data | 8ymkMC 8ymjC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_39396.map.gz / Format: CCP4 / Size: 91.1 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: 1.06 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_39396_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: Localized reconstruction from dataset A, generated by CryoSPARC...
File | emd_39396_additional_1.map | ||||||||||||
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Annotation | Localized reconstruction from dataset A, generated by CryoSPARC local refinement job, and then resampled on the dataset A0 map (main map of this entry) in UCSF Chimera. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_39396_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_39396_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Hepatitis B virus ayw/China/Tibet127/2002
Entire | Name: Hepatitis B virus ayw/China/Tibet127/2002 |
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Components |
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-Supramolecule #1: Hepatitis B virus ayw/China/Tibet127/2002
Supramolecule | Name: Hepatitis B virus ayw/China/Tibet127/2002 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 489469 / Sci species name: Hepatitis B virus ayw/China/Tibet127/2002 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: SEROTYPE / Virus enveloped: Yes / Virus empty: Yes |
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-Macromolecule #1: Isoform S of Large envelope protein
Macromolecule | Name: Isoform S of Large envelope protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Hepatitis B virus ayw/China/Tibet127/2002 / Strain: isolate China/Tibet127/2002 |
Molecular weight | Theoretical: 25.408059 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MENITSGFLG PLLVLQAGFF LLTRILTIPQ SLDSWWTSLN FLGGTTVCLG QNSQSPISNH SPTSCPPTCP GYRWMCLRRF IIFLFILLL CLIFLLVLLD YQGMLPVCPL IPGSSTTSTG PCRTCTTPAQ GTSMYPSCCC TKPSDGNCTC IPIPSSWAFG K FLWEWASA ...String: MENITSGFLG PLLVLQAGFF LLTRILTIPQ SLDSWWTSLN FLGGTTVCLG QNSQSPISNH SPTSCPPTCP GYRWMCLRRF IIFLFILLL CLIFLLVLLD YQGMLPVCPL IPGSSTTSTG PCRTCTTPAQ GTSMYPSCCC TKPSDGNCTC IPIPSSWAFG K FLWEWASA RFSWLSLLVP FVQWFVGLSP TVWLSVIWMM WYWGPSLYSI LSPFLPLLPI FFCLWVYI UniProtKB: Large envelope protein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Grid | Model: Quantifoil R0.6/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: OTHER |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 50 / Number real images: 157206 / Average exposure time: 3.0 sec. / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 22500 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Initial model | PDB ID: Chain - Chain ID: A / Chain - Source name: PDB / Chain - Initial model type: experimental model |
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Refinement | Space: REAL / Protocol: RIGID BODY FIT |
Output model | PDB-8ymk: |