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- EMDB-23665: Structural basis for SARS-CoV-2 envelope protein in recognition o... -
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Basic information
Entry | Database: EMDB / ID: EMD-23665 | |||||||||
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Title | Structural basis for SARS-CoV-2 envelope protein in recognition of human cell junction protein PALS1 | |||||||||
![]() | Cryosparc non-uniform refinement without sharpening | |||||||||
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![]() | SARS-CoV-2 envelope protein / PDZ-binding motif / complex / pathogen-host interaction / CELL ADHESION-VIRAL PROTEIN complex | |||||||||
Function / homology | ![]() disruption of cellular anatomical structure in another organism / protein localization to myelin sheath abaxonal region / SARS-CoV-1 targets PDZ proteins in cell-cell junction / viral budding from Golgi membrane / establishment or maintenance of polarity of embryonic epithelium / myelin assembly / morphogenesis of an epithelial sheet / Tight junction interactions / SARS-CoV-2 targets PDZ proteins in cell-cell junction / cytoplasmic capsid assembly ...disruption of cellular anatomical structure in another organism / protein localization to myelin sheath abaxonal region / SARS-CoV-1 targets PDZ proteins in cell-cell junction / viral budding from Golgi membrane / establishment or maintenance of polarity of embryonic epithelium / myelin assembly / morphogenesis of an epithelial sheet / Tight junction interactions / SARS-CoV-2 targets PDZ proteins in cell-cell junction / cytoplasmic capsid assembly / lateral loop / myelin sheath adaxonal region / regulation of transforming growth factor beta receptor signaling pathway / Regulation of gap junction activity / Schmidt-Lanterman incisure / peripheral nervous system myelin maintenance / establishment or maintenance of epithelial cell apical/basal polarity / apical junction complex / generation of neurons / central nervous system neuron development / host cell Golgi membrane / endoplasmic reticulum-Golgi intermediate compartment / bicellular tight junction / Maturation of protein E / endoplasmic reticulum-Golgi intermediate compartment membrane / protein localization to plasma membrane / adherens junction / cerebral cortex development / monoatomic ion channel activity / gene expression / perikaryon / Translation of Structural Proteins / Virion Assembly and Release / Induction of Cell-Cell Fusion / structural constituent of virion / Attachment and Entry / apical plasma membrane / protein domain specific binding / axon / SARS-CoV-2 activates/modulates innate and adaptive immune responses / virion membrane / Golgi apparatus / protein-containing complex / extracellular exosome / ATP binding / identical protein binding / membrane / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.65 Å | |||||||||
![]() | Liu Q / Chai J | |||||||||
![]() | ![]() Title: Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1. Authors: Jin Chai / Yuanheng Cai / Changxu Pang / Liguo Wang / Sean McSweeney / John Shanklin / Qun Liu / ![]() Abstract: The COVID-19 pandemic, caused by the SARS-CoV-2 virus, has created global health and economic emergencies. SARS-CoV-2 viruses promote their own spread and virulence by hijacking human proteins, which ...The COVID-19 pandemic, caused by the SARS-CoV-2 virus, has created global health and economic emergencies. SARS-CoV-2 viruses promote their own spread and virulence by hijacking human proteins, which occurs through viral protein recognition of human targets. To understand the structural basis for SARS-CoV-2 viral-host protein recognition, here we use cryo-electron microscopy (cryo-EM) to determine a complex structure of the human cell junction protein PALS1 and SARS-CoV-2 viral envelope (E) protein. Our reported structure shows that the E protein C-terminal DLLV motif recognizes a pocket formed exclusively by hydrophobic residues from the PDZ and SH3 domains of PALS1. Our structural analysis provides an explanation for the observation that the viral E protein recruits PALS1 from lung epithelial cell junctions. In addition, our structure provides novel targets for peptide- and small-molecule inhibitors that could block the PALS1-E interactions to reduce E-mediated virulence. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 31.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.9 KB 9.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 6.4 KB | Display | ![]() |
Images | ![]() | 152.4 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 474.8 KB | Display | ![]() |
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Full document | ![]() | 474.3 KB | Display | |
Data in XML | ![]() | 9.8 KB | Display | |
Data in CIF | ![]() | 12.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7m4rMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Cryosparc non-uniform refinement without sharpening | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.684 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Complex structure of SARS-CoV-2 envelope protein Ec18 and human P...
Entire | Name: Complex structure of SARS-CoV-2 envelope protein Ec18 and human PALS1 PSG domains |
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Components |
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-Supramolecule #1: Complex structure of SARS-CoV-2 envelope protein Ec18 and human P...
Supramolecule | Name: Complex structure of SARS-CoV-2 envelope protein Ec18 and human PALS1 PSG domains type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: MAGUK p55 subfamily member 5
Macromolecule | Name: MAGUK p55 subfamily member 5 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 44.780504 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SNAPITDERV YESIGQYGGE TVKIVRIEKA RDIPLGATVR NEMDSVIISR IVKGGAAEKS GLLHEGDEVL EINGIEIRGK DVNEVFDLL SDMHGTLTFV LIPSQQIKPP PAKETVIHVK AHFDYDPSDD PYVPCRELGL SFQKGDILHV ISQEDPNWWQ A YREGDEDN ...String: SNAPITDERV YESIGQYGGE TVKIVRIEKA RDIPLGATVR NEMDSVIISR IVKGGAAEKS GLLHEGDEVL EINGIEIRGK DVNEVFDLL SDMHGTLTFV LIPSQQIKPP PAKETVIHVK AHFDYDPSDD PYVPCRELGL SFQKGDILHV ISQEDPNWWQ A YREGDEDN QPLAGLVPGK EEILTYEEMS LYHQPANRKR PIILIGPQNC GQNELRQRLM NKEKDRFASA VPHTTRSRRD QE VAGRDYH FVSRQAFEAD IAAGKFIEHG EFEKNLYGTS IDSVRQVINS GKICLLSLRT QSLKTLRNSD LKPYIIFIAP PSQ ERLRAL LAKEGKNPKP EELREIIEKT REMEQNNGHY FDTAIVNSDL DKAYQELLRL INKLDTEPQW VPSTWLR UniProtKB: Protein PALS1, Protein PALS1 |
-Macromolecule #2: Envelope small membrane protein
Macromolecule | Name: Envelope small membrane protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 2.062395 KDa |
Sequence | String: VYSRVKNLNS SRVPDLLV UniProtKB: Envelope small membrane protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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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 BIOQUANTUM (6k x 4k) / Average electron dose: 64.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |