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Yorodumi- EMDB-11076: Tomogram of influenza A/Hong Kong/1/1968 virus like particles (HA... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11076 | ||||||||||||
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Title | Tomogram of influenza A/Hong Kong/1/1968 virus like particles (HA,NA,M1,M2) | ||||||||||||
Map data | Tomograms showing a influenza A/HK68 virus like particle | ||||||||||||
Sample |
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Biological species | Influenza A virus | ||||||||||||
Method | electron tomography / cryo EM | ||||||||||||
Authors | Peukes J / Xiong X / Erlendsson S / Qu K / Wan W / Kraeusslich H-G / Briggs JAG | ||||||||||||
Funding support | European Union, Germany, United Kingdom, 3 items
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Citation | Journal: Nature / Year: 2020 Title: The native structure of the assembled matrix protein 1 of influenza A virus. Authors: Julia Peukes / Xiaoli Xiong / Simon Erlendsson / Kun Qu / William Wan / Leslie J Calder / Oliver Schraidt / Susann Kummer / Stefan M V Freund / Hans-Georg Kräusslich / John A G Briggs / Abstract: Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by ...Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by forming an endoskeleton beneath the virus membrane. The structure of full-length M1, and how it oligomerizes to mediate the assembly of virions, is unknown. Here we determine the complete structure of assembled M1 within intact virus particles, as well as the structure of M1 oligomers reconstituted in vitro. We find that the C-terminal domain of M1 is disordered in solution but can fold and bind in trans to the N-terminal domain of another M1 monomer, thus polymerizing M1 into linear strands that coat the interior surface of the membrane of the assembling virion. In the M1 polymer, five histidine residues-contributed by three different monomers of M1-form a cluster that can serve as the pH-sensitive disassembly switch after entry into a target cell. These structures therefore reveal mechanisms of influenza virus assembly and disassembly. | ||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_11076.map.gz | 726.1 MB | EMDB map data format | |
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Header (meta data) | emd-11076-v30.xml emd-11076.xml | 11.1 KB 11.1 KB | Display Display | EMDB header |
Images | emd_11076.png | 146.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11076 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11076 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_11076.map.gz / Format: CCP4 / Size: 788.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Tomograms showing a influenza A/HK68 virus like particle | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 7.12 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Influenza A virus
Entire | Name: Influenza A virus |
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Components |
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-Supramolecule #1: Influenza A virus
Supramolecule | Name: Influenza A virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1 Details: virus like particles were formed by expressing plasmids coding for a subset (HA,NA,M1,M2) of the viral proteins NCBI-ID: 11320 / Sci species name: Influenza A virus / Sci species strain: A/Hong Kong/1/1968 (H3N2) / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: OTHER / Virus enveloped: Yes / Virus empty: Yes |
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Host (natural) | Organism: Homo sapiens (human) |
Host system | Organism: Homo sapiens (human) / Recombinant cell: HEK293-T |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | electron tomography |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil R2/2 / Material: GOLD / Mesh: 200 / Support film - Material: CARBON / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Instrument: LEICA EM GP |
Sectioning | Other: NO SECTIONING |
Fiducial marker | Manufacturer: um / Diameter: 10 nm |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 2.5 µm / Nominal magnification: 81000 |
Specialist optics | Energy filter - Name: GIF Quantum LS / 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: SUPER-RESOLUTION / Average electron dose: 2.9 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Algorithm: BACK PROJECTION / Software - Name: eTomo / Number images used: 40 |
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