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Yorodumi- EMDB-31978: SARS-CoV-2 M protein dimer (short form) in complex with YN7717_9 Fab -
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Open data
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Basic information
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| Title | SARS-CoV-2 M protein dimer (short form) in complex with YN7717_9 Fab | |||||||||
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Sample |
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Keywords | SARS-CoV-2 / M protein / viral structural protein / virus assembly / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex | |||||||||
| Function / homology | Function and homology informationMaturation of protein M / SARS-CoV-2 modulates autophagy / host cell Golgi membrane / CD28 dependent PI3K/Akt signaling / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / protein sequestering activity / VEGFR2 mediated vascular permeability / PIP3 activates AKT signaling / TRAF3-dependent IRF activation pathway ...Maturation of protein M / SARS-CoV-2 modulates autophagy / host cell Golgi membrane / CD28 dependent PI3K/Akt signaling / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / protein sequestering activity / VEGFR2 mediated vascular permeability / PIP3 activates AKT signaling / TRAF3-dependent IRF activation pathway / Translation of Structural Proteins / Virion Assembly and Release / Induction of Cell-Cell Fusion / structural constituent of virion / Attachment and Entry / viral envelope / SARS-CoV-2 activates/modulates innate and adaptive immune responses / virion membrane / identical protein binding / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
Authors | Zhang Z / Ohto U / Shimizu T | |||||||||
| Funding support | 1 items
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Citation | Journal: Nat Commun / Year: 2022Title: Structure of SARS-CoV-2 membrane protein essential for virus assembly. Authors: Zhikuan Zhang / Norimichi Nomura / Yukiko Muramoto / Toru Ekimoto / Tomoko Uemura / Kehong Liu / Moeko Yui / Nozomu Kono / Junken Aoki / Mitsunori Ikeguchi / Takeshi Noda / So Iwata / ...Authors: Zhikuan Zhang / Norimichi Nomura / Yukiko Muramoto / Toru Ekimoto / Tomoko Uemura / Kehong Liu / Moeko Yui / Nozomu Kono / Junken Aoki / Mitsunori Ikeguchi / Takeshi Noda / So Iwata / Umeharu Ohto / Toshiyuki Shimizu / ![]() Abstract: The coronavirus membrane protein (M) is the most abundant viral structural protein and plays a central role in virus assembly and morphogenesis. However, the process of M protein-driven virus ...The coronavirus membrane protein (M) is the most abundant viral structural protein and plays a central role in virus assembly and morphogenesis. However, the process of M protein-driven virus assembly are largely unknown. Here, we report the cryo-electron microscopy structure of the SARS-CoV-2 M protein in two different conformations. M protein forms a mushroom-shaped dimer, composed of two transmembrane domain-swapped three-helix bundles and two intravirion domains. M protein further assembles into higher-order oligomers. A highly conserved hinge region is key for conformational changes. The M protein dimer is unexpectedly similar to SARS-CoV-2 ORF3a, a viral ion channel. Moreover, the interaction analyses of M protein with nucleocapsid protein (N) and RNA suggest that the M protein mediates the concerted recruitment of these components through the positively charged intravirion domain. Our data shed light on the M protein-driven virus assembly mechanism and provide a structural basis for therapeutic intervention targeting M protein. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_31978.map.gz | 27.6 MB | EMDB map data format | |
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| Header (meta data) | emd-31978-v30.xml emd-31978.xml | 15.2 KB 15.2 KB | Display Display | EMDB header |
| Images | emd_31978.png | 65.3 KB | ||
| Filedesc metadata | emd-31978.cif.gz | 6.2 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31978 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31978 | HTTPS FTP |
-Validation report
| Summary document | emd_31978_validation.pdf.gz | 497.3 KB | Display | EMDB validaton report |
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| Full document | emd_31978_full_validation.pdf.gz | 496.9 KB | Display | |
| Data in XML | emd_31978_validation.xml.gz | 6.1 KB | Display | |
| Data in CIF | emd_31978_validation.cif.gz | 7.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31978 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31978 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7vgsMC ![]() 7vgrC 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 |
| EM raw data | EMPIAR-11168 (Title: Structure of SARS-CoV-2 membrane protein / Data size: 4.4 TB / Data #1: M protein (LMNG/CHS) [micrographs - multiframe]Data #2: M protein (LMNG/CHS) + Fab-E [micrographs - multiframe] Data #3: M protein (LMNG/CHS) + Fab-B [micrographs - multiframe]) |
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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_31978.map.gz / Format: CCP4 / Size: 52.7 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: 1.245 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : SARS-CoV-2 M protein dimer (short form) in complex with YN7717_9 Fab
| Entire | Name: SARS-CoV-2 M protein dimer (short form) in complex with YN7717_9 Fab |
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| Components |
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-Supramolecule #1: SARS-CoV-2 M protein dimer (short form) in complex with YN7717_9 Fab
| Supramolecule | Name: SARS-CoV-2 M protein dimer (short form) in complex with YN7717_9 Fab type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #2: Membrane protein
| Supramolecule | Name: Membrane protein / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Supramolecule #3: YN7717_9 Fab
| Supramolecule | Name: YN7717_9 Fab / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Membrane protein
| Macromolecule | Name: Membrane protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 28.257822 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MHHHHHHHHD YKDDDDKENL YFQGMADSNG TITVEELKKL LEQWNLVIGF LFLTWICLLQ FAYANRNRFL YIIKLIFLWL LWPVTLACF VLAAVYRINW ITGGIAIAMA CLVGLMWLSY FIASFRLFAR TRSMWSFNPE TNILLNVPLH GTILTRPLLE S ELVIGAVI ...String: MHHHHHHHHD YKDDDDKENL YFQGMADSNG TITVEELKKL LEQWNLVIGF LFLTWICLLQ FAYANRNRFL YIIKLIFLWL LWPVTLACF VLAAVYRINW ITGGIAIAMA CLVGLMWLSY FIASFRLFAR TRSMWSFNPE TNILLNVPLH GTILTRPLLE S ELVIGAVI LRGHLRIAGH HLGRCDIKDL PKEITVATSR TLSYYKLGAS QRVAGDSGFA AYSRYRIGNY KLNTDHSSSS DN IALLVQ UniProtKB: Membrane protein |
-Macromolecule #2: YN7717_9 Fab light chain
| Macromolecule | Name: YN7717_9 Fab light chain / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 23.999266 KDa |
| Sequence | String: DIVMTQSPAS LAVSLGQRAT ISCKASQSID YDGDNYMNWY QQKPGQPPKL LIYTTSNLES GIPARFSGSG SGTDFTLNIH PVEEGDAAT YYCQQNNEDP YTFGGGTKLE IKRADAAPTV SIFPPSSEQL TSGGASVVCF LNNFYPKDIN VKWKIDGSER Q NGVLNSWT ...String: DIVMTQSPAS LAVSLGQRAT ISCKASQSID YDGDNYMNWY QQKPGQPPKL LIYTTSNLES GIPARFSGSG SGTDFTLNIH PVEEGDAAT YYCQQNNEDP YTFGGGTKLE IKRADAAPTV SIFPPSSEQL TSGGASVVCF LNNFYPKDIN VKWKIDGSER Q NGVLNSWT DQDSKDSTYS MSSTLTLTKD EYERHNSYTC EATHKTSTSP IVKSFNRNEC |
-Macromolecule #3: YN7717_9 Fab heavy chain
| Macromolecule | Name: YN7717_9 Fab heavy chain / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 24.499639 KDa |
| Sequence | String: EVQLQQSGPE LVKPGASMKI SCKTSGYSFT GYTMNWVKQS HGKNLEWIGL INPYNGDTSY NQKFKGKATL TVDKSSSTAY MELLSLTSE DSAVYYCEVI NTYWGQGTLV TVSAAKTTPP SVYPLAPGSA AQTNSMVTLG CLVKGYFPEP VTVTWNSGSL S SGVHTFPA ...String: EVQLQQSGPE LVKPGASMKI SCKTSGYSFT GYTMNWVKQS HGKNLEWIGL INPYNGDTSY NQKFKGKATL TVDKSSSTAY MELLSLTSE DSAVYYCEVI NTYWGQGTLV TVSAAKTTPP SVYPLAPGSA AQTNSMVTLG CLVKGYFPEP VTVTWNSGSL S SGVHTFPA VLQSDLYTLS SSVTVPSSTW PSETVTCNVA HPASSTKVDK KIVPRDCGCK PCICTVPEVS S |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1.5 mg/mL |
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| Buffer | pH: 7.6 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 61.4 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-7vgs: |
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Homo sapiens (human)
FIELD EMISSION GUN
