+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-10697 | |||||||||
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Title | Ectodomain of X-31 Haemagglutinin at pH 5 (State I) | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Haemagglutinin / Hemagglutinin / Fusion protein / VIRAL PROTEIN | |||||||||
Function / homology | Function and homology information viral 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 | unidentified influenza virus | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
Authors | Benton DJ / Rosenthal PB | |||||||||
Funding support | United Kingdom, 2 items
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Citation | Journal: Nature / Year: 2020 Title: Structural transitions in influenza haemagglutinin at membrane fusion pH. Authors: Donald J Benton / Steven J Gamblin / Peter B Rosenthal / John J Skehel / Abstract: Infection by enveloped viruses involves fusion of their lipid envelopes with cellular membranes to release the viral genome into cells. For HIV, Ebola, influenza and numerous other viruses, envelope ...Infection by enveloped viruses involves fusion of their lipid envelopes with cellular membranes to release the viral genome into cells. For HIV, Ebola, influenza and numerous other viruses, envelope glycoproteins bind the infecting virion to cell-surface receptors and mediate membrane fusion. In the case of influenza, the receptor-binding glycoprotein is the haemagglutinin (HA), and following receptor-mediated uptake of the bound virus by endocytosis, it is the HA that mediates fusion of the virus envelope with the membrane of the endosome. Each subunit of the trimeric HA consists of two disulfide-linked polypeptides, HA1 and HA2. The larger, virus-membrane-distal, HA1 mediates receptor binding; the smaller, membrane-proximal, HA2 anchors HA in the envelope and contains the fusion peptide, a region that is directly involved in membrane interaction. The low pH of endosomes activates fusion by facilitating irreversible conformational changes in the glycoprotein. The structures of the initial HA at neutral pH and the final HA at fusion pH have been investigated by electron microscopy and X-ray crystallography. Here, to further study the process of fusion, we incubate HA for different times at pH 5.0 and directly image structural changes using single-particle cryo-electron microscopy. We describe three distinct, previously undescribed forms of HA, most notably a 150 Å-long triple-helical coil of HA2, which may bridge between the viral and endosomal membranes. Comparison of these structures reveals concerted conformational rearrangements through which the HA mediates membrane fusion. | |||||||||
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_10697.map.gz | 2.1 MB | EMDB map data format | |
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Header (meta data) | emd-10697-v30.xml emd-10697.xml | 17.2 KB 17.2 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_10697_fsc.xml | 14.2 KB | Display | FSC data file |
Images | emd_10697.png | 126.6 KB | ||
Masks | emd_10697_msk_1.map | 244.1 MB | Mask map | |
Filedesc metadata | emd-10697.cif.gz | 5.8 KB | ||
Others | emd_10697_half_map_1.map.gz emd_10697_half_map_2.map.gz | 226.4 MB 226.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-10697 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-10697 | HTTPS FTP |
-Validation report
Summary document | emd_10697_validation.pdf.gz | 666.1 KB | Display | EMDB validaton report |
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Full document | emd_10697_full_validation.pdf.gz | 665.6 KB | Display | |
Data in XML | emd_10697_validation.xml.gz | 22.4 KB | Display | |
Data in CIF | emd_10697_validation.cif.gz | 28.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-10697 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-10697 | HTTPS FTP |
-Related structure data
Related structure data | 6y5hMC 6y5gC 6y5iC 6y5jC 6y5kC 6y5lC 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_10697.map.gz / Format: CCP4 / Size: 244.1 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: 1.09 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_10697_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_10697_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_10697_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : X-31 Influenza Haemagglutinin
Entire | Name: X-31 Influenza Haemagglutinin |
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Components |
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-Supramolecule #1: X-31 Influenza Haemagglutinin
Supramolecule | Name: X-31 Influenza Haemagglutinin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: unidentified influenza virus |
Molecular weight | Theoretical: 164 KDa |
-Macromolecule #1: X-31 Influenza Haemagglutinin HA1
Macromolecule | Name: X-31 Influenza Haemagglutinin HA1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: unidentified influenza virus |
Molecular weight | Theoretical: 34.967324 KDa |
Recombinant expression | Organism: Gallus gallus (chicken) |
Sequence | String: NSTATLCLGH HAVPNGTLVK TITDDQIEVT NATELVQSSS TGKICNNPHR ILDGIDCTLI DALLGDPHCD VFQNETWDLF VERSKAFSN CYPYDVPDYA SLRSLVASSG TLEFITEGFT WTGVTQNGGS NACKRGPGSG FFSRLNWLTK SGSTYPVLNV T MPNNDNFD ...String: NSTATLCLGH HAVPNGTLVK TITDDQIEVT NATELVQSSS TGKICNNPHR ILDGIDCTLI DALLGDPHCD VFQNETWDLF VERSKAFSN CYPYDVPDYA SLRSLVASSG TLEFITEGFT WTGVTQNGGS NACKRGPGSG FFSRLNWLTK SGSTYPVLNV T MPNNDNFD KLYIWGIHHP STNQEQTSLY VQASGRVTVS TRRSQQTIIP NIGSRPWVRG LSSRISIYWT IVKPGDVLVI NS NGNLIAP RGYFKMRTGK SSIMRSDAPI DTCISECITP NGSIPNDKPF QNVNKITYGA CPKYVKQNTL KLATGMRNVP E UniProtKB: Hemagglutinin |
-Macromolecule #2: X-31 Influenza Haemagglutinin HA2
Macromolecule | Name: X-31 Influenza Haemagglutinin HA2 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: unidentified influenza virus |
Molecular weight | Theoretical: 19.912959 KDa |
Recombinant expression | Organism: Gallus gallus (chicken) |
Sequence | String: GLFGAIAGFI ENGWEGMIDG WYGFRHQNSE GTGQAADLKS TQAAIDQING KLNRVIEKTN EKFHQIEKEF SEVEGRIQDL EKYVEDTKI DLWSYNAELL VALENQHTID LTDSEMNKLF EKTRRQLREN AEEMGNGCFK IYHKCDNACI ESIRNGTYDH D VYRDEALN NRFQ UniProtKB: Hemagglutinin |
-Macromolecule #5: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 5 / Number of copies: 6 / 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 |
-Sample preparation
Concentration | 1.25 mg/mL |
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Buffer | pH: 5 |
Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK III |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average exposure time: 60.0 sec. / Average electron dose: 33.9 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |