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Open data
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Basic information
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| Title | The cryoEM structure of H5N8 HA in an auto inhibited state | |||||||||
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Sample |
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Keywords | Influenza / glycosylation / sialic acid / VIRAL PROTEIN | |||||||||
| Function / homology | Function and homology informationviral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane Similarity search - Function | |||||||||
| Biological species | ![]() Influenza A virus | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
Authors | Li R / Gao J / Wang L / Gui M / Xiang Y | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Npj Viruses / Year: 2024Title: Multivalent interactions between fully glycosylated influenza virus hemagglutinins mediated by glycans at distinct N-glycosylation sites. Authors: Ruofan Li / Jingjing Gao / Lin Wang / Miao Gui / Ye Xiang / ![]() Abstract: The hemagglutinin (HA) glycoprotein of influenza virus binds host cell receptors and mediates viral entry. Here we present cryo-EM structures of fully glycosylated HAs from H5N1 and H5N8 influenza ...The hemagglutinin (HA) glycoprotein of influenza virus binds host cell receptors and mediates viral entry. Here we present cryo-EM structures of fully glycosylated HAs from H5N1 and H5N8 influenza viruses. We find that the H5N1 HA can form filaments that comprise two head-to-head HA trimers. Multivalent interactions between the two HA trimers are mediated by glycans attached to N158. The distal Sia1-Gal2-NAG3 sugar moiety of N158 interacts with the receptor binding site on the opposing HA trimer. Additional interactions are observed between NAG3 and residues K222 and K193. The H5N8 HA lacks the N158 glycosylation site and does not form the filamentous structure. However, the H5N8 HA exhibits an auto-inhibition conformation, where the receptor binding site is occupied by the glycan chain attached to residue N169 from a neighboring protomer. These structures represent native HA-glycan interactions, which may closely mimic the receptor-HA interactions on the cell surface. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_60014.map.gz | 59.7 MB | EMDB map data format | |
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| Header (meta data) | emd-60014-v30.xml emd-60014.xml | 19.5 KB 19.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_60014_fsc.xml | 8.4 KB | Display | FSC data file |
| Images | emd_60014.png | 30.1 KB | ||
| Filedesc metadata | emd-60014.cif.gz | 6.9 KB | ||
| Others | emd_60014_half_map_1.map.gz emd_60014_half_map_2.map.gz | 59.4 MB 59.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-60014 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-60014 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8zdvMC ![]() 8zdwC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_60014.map.gz / Format: CCP4 / Size: 64 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: 1.0742 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_60014_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_60014_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : H5N8 HA ectodomain
| Entire | Name: H5N8 HA ectodomain |
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| Components |
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-Supramolecule #1: H5N8 HA ectodomain
| Supramolecule | Name: H5N8 HA ectodomain / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() Influenza A virus / Strain: A/chicken/Czech_Republic/1566-1/2021 |
| Molecular weight | Theoretical: 200 KDa |
-Macromolecule #1: Hemagglutinin
| Macromolecule | Name: Hemagglutinin / type: protein_or_peptide / ID: 1 Details: The depositor states that 'For the sequence issues, we only have the GISAID ID: EPI_ISL_977513, since it is not uploaded to uniprot database.' Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Influenza A virus |
| Molecular weight | Theoretical: 37.793035 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MENIVLLLAI VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE KTHNGKLCDL NGVKPLILKD CSVAGWLLGN PMCDEFIRV PEWSYIVERA NPSNDLCYPG SLNDYEELKH LLSRINHFEK ILIIPKSSWP NHETSLGVSA ACPYQGAPSF F RNVVWLIK ...String: MENIVLLLAI VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE KTHNGKLCDL NGVKPLILKD CSVAGWLLGN PMCDEFIRV PEWSYIVERA NPSNDLCYPG SLNDYEELKH LLSRINHFEK ILIIPKSSWP NHETSLGVSA ACPYQGAPSF F RNVVWLIK KNDAYPTIKI SYNNTNQEDL LILWGIHHSN NAEEQTNLYK NPTTYISVGT STLNQRLVPK IATRSQVNGQ RG RMDFFWT ILKPDDAIHF ESNGNFIAPE YAYKIVKKGD STIMKSGVEY GHCNTKCQTP VGAINSSMPF HNIHPLTIGE CPK YVKSNK LVLATGLRNS UniProtKB: Hemagglutinin |
-Macromolecule #2: Hemagglutinin
| Macromolecule | Name: Hemagglutinin / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Influenza A virus |
| Molecular weight | Theoretical: 21.995514 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: PLREKRRKRG LFGAIAGFIE GGWQGMVDGW YGYHHSNEQG SGYAADKEST QKAIDGVTNK VNSIIDKMNT QFEAVGREFN NLERRIENL NKKMEDGFLD VWTYNAELLV LMENERTLDF HDSNVKNLYD KVRLQLRDNA KELGNGCFEF YHKCDNECME S VRNGTYDY PQYSGEARLK REEISGVKLE SI UniProtKB: Hemagglutinin |
-Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 12 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-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: 8 |
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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: 2.5 µm / Nominal defocus min: 1.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Influenza A virus
Authors
China, 1 items
Citation














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




































Homo sapiens (human)
Processing
FIELD EMISSION GUN


