+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11108 | |||||||||||||||
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Title | The atomic structure of HAdV-F41 at pH 7.4 | |||||||||||||||
Map data | Full map masked | |||||||||||||||
Sample |
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Function / homology | Function and homology information hexon binding / viral capsid, decoration / T=25 icosahedral viral capsid / lysis of host organelle involved in viral entry into host cell / viral procapsid / virion component => GO:0044423 / host cell nucleolus / microtubule-dependent intracellular transport of viral material towards nucleus / viral release from host cell / endocytosis involved in viral entry into host cell ...hexon binding / viral capsid, decoration / T=25 icosahedral viral capsid / lysis of host organelle involved in viral entry into host cell / viral procapsid / virion component => GO:0044423 / host cell nucleolus / microtubule-dependent intracellular transport of viral material towards nucleus / viral release from host cell / endocytosis involved in viral entry into host cell / viral capsid / host cell cytoplasm / symbiont entry into host cell / host cell nucleus / virion attachment to host cell / structural molecule activity / DNA binding Similarity search - Function | |||||||||||||||
Biological species | HAdV-41 (virus) / Human adenovirus 41 | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.77 Å | |||||||||||||||
Authors | Carlson L-A / Rafie K | |||||||||||||||
Funding support | Sweden, 4 items
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Citation | Journal: Sci Adv / Year: 2021 Title: The structure of enteric human adenovirus 41-A leading cause of diarrhea in children. Authors: K Rafie / A Lenman / J Fuchs / A Rajan / N Arnberg / L-A Carlson / Abstract: Human adenovirus (HAdV) types F40 and F41 are a prominent cause of diarrhea and diarrhea-associated mortality in young children worldwide. These enteric HAdVs differ notably in tissue tropism and ...Human adenovirus (HAdV) types F40 and F41 are a prominent cause of diarrhea and diarrhea-associated mortality in young children worldwide. These enteric HAdVs differ notably in tissue tropism and pathogenicity from respiratory and ocular adenoviruses, but the structural basis for this divergence has been unknown. Here, we present the first structure of an enteric HAdV-HAdV-F41-determined by cryo-electron microscopy to a resolution of 3.8 Å. The structure reveals extensive alterations to the virion exterior as compared to nonenteric HAdVs, including a unique arrangement of capsid protein IX. The structure also provides new insights into conserved aspects of HAdV architecture such as a proposed location of core protein V, which links the viral DNA to the capsid, and assembly-induced conformational changes in the penton base protein. Our findings provide the structural basis for adaptation of enteric HAdVs to a fundamentally different tissue tropism. | |||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_11108.map.gz | 934 MB | EMDB map data format | |
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Header (meta data) | emd-11108-v30.xml emd-11108.xml | 29.8 KB 29.8 KB | Display Display | EMDB header |
Images | emd_11108.png | 173.6 KB | ||
Masks | emd_11108_msk_1.map | 2.7 GB | Mask map | |
Others | emd_11108_additional_1.map.gz emd_11108_half_map_1.map.gz emd_11108_half_map_2.map.gz | 40.8 MB 2.5 GB 2.5 GB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11108 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11108 | HTTPS FTP |
-Related structure data
Related structure data | 6z7nMC 6z7qC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_11108.map.gz / Format: CCP4 / Size: 2.7 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Full map masked | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.041 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_11108_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: ASU map for model building
File | emd_11108_additional_1.map | ||||||||||||
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Annotation | ASU map for model building | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half 1
File | emd_11108_half_map_1.map | ||||||||||||
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Annotation | Half 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half 2
File | emd_11108_half_map_2.map | ||||||||||||
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Annotation | Half 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Human adenovirus 41
+Supramolecule #1: Human adenovirus 41
+Macromolecule #1: Pre-protein VI
+Macromolecule #2: Hexon protein
+Macromolecule #3: Penton protein
+Macromolecule #4: Core-capsid bridging protein
+Macromolecule #5: Pre-hexon-linking protein IIIa
+Macromolecule #6: Hexon-interlacing protein
+Macromolecule #7: Pre-hexon-linking protein VIII
+Macromolecule #8: Fiber protein
+Macromolecule #9: Unknown
+Macromolecule #10: Unknown
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 4.2 mg/mL |
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Buffer | pH: 7.4 Details: PBS buffer made from comemrcial PBS tablets Medicargo, PBS tablets, 09-9400-100 |
Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: OTHER / Pretreatment - Pressure: 0.037 kPa |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 80 % / Chamber temperature: 295.15 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 130000 |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 1-40 / Number grids imaged: 2 / Number real images: 6929 / Average electron dose: 1.03 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Particle selection | Number selected: 25667 |
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CTF correction | Software - Name: Gctf (ver. 1.18) / Software - details: icle CTF correction |
Startup model | Type of model: EMDB MAP EMDB ID: |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0-beta) |
Final 3D classification | Software - Name: RELION (ver. 3.0-beta) |
Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0-beta) |
Final reconstruction | Applied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 3.77 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0-beta) / Number images used: 19472 |