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- EMDB-30038: Cryo-EM structures of SADS-CoV spike glycoproteins -

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Basic information

Entry
Database: EMDB / ID: EMD-30038
TitleCryo-EM structures of SADS-CoV spike glycoproteins
Map data
Sample
  • Complex: SADS-CoV glycoprotein
    • Protein or peptide: Spike glycoproteinSpike protein
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
Function / homology
Function and homology information


: / host cell membrane / endocytosis involved in viral entry into host cell / receptor-mediated virion attachment to host cell / membrane => GO:0016020 / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion membrane
Similarity search - Function
Spike glycoprotein S2, coronavirus, C-terminal / Coronavirus spike glycoprotein S2, intravirion / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2 / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal
Similarity search - Domain/homology
Biological speciesSwine acute diarrhea syndrome coronavirus
Methodsingle particle reconstruction / cryo EM / Resolution: 2.83 Å
AuthorsWang X / Yu J / Qiao S / Guo R
CitationJournal: Nat Commun / Year: 2020
Title: Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution.
Authors: Jinfang Yu / Shuyuan Qiao / Runyu Guo / Xinquan Wang /
Abstract: Porcine coronavirus SADS-CoV has been identified from suckling piglets with severe diarrhea in southern China in 2017. The SADS-CoV genome shares ~95% identity to that of bat α-coronavirus HKU2, ...Porcine coronavirus SADS-CoV has been identified from suckling piglets with severe diarrhea in southern China in 2017. The SADS-CoV genome shares ~95% identity to that of bat α-coronavirus HKU2, suggesting that SADS-CoV may have emerged from a natural reservoir in bats. Here we report the cryo-EM structures of HKU2 and SADS-CoV spike (S) glycoprotein trimers at 2.38 Å and 2.83 Å resolution, respectively. We systematically compare the domains of HKU2 spike with those of α-, β-, γ-, and δ-coronavirus spikes, showing that the S1 subunit N- and C-terminal domains of HKU2/SADS-CoV are ancestral domains in the evolution of coronavirus spike proteins. The connecting region after the fusion peptide in the S2 subunit of HKU2/SADS-CoV adopts a unique conformation. These results structurally demonstrate a close evolutionary relationship between HKU2/SADS-CoV and β-coronavirus spikes and provide insights into the evolution and cross-species transmission of coronaviruses.
History
DepositionFeb 24, 2020-
Header (metadata) releaseMay 27, 2020-
Map releaseMay 27, 2020-
UpdateJul 29, 2020-
Current statusJul 29, 2020Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.03
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  • Surface view with fitted model
  • Atomic models: PDB-6m16
  • Surface level: 0.025
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_30038.png

Downloads & links

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Map

FileDownload / File: emd_30038.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.061 Å
Density
Contour LevelBy AUTHOR: 0.0201 / Movie #1: 0.03
Minimum - Maximum-0.15030831 - 0.20914844
Average (Standard dev.)0.0004109978 (±0.0057185814)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 271.616 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0611.0611.061
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z271.616271.616271.616
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ280280280
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.1500.2090.000

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Supplemental data

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Sample components

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Entire : SADS-CoV glycoprotein

EntireName: SADS-CoV glycoprotein
Components
  • Complex: SADS-CoV glycoprotein
    • Protein or peptide: Spike glycoproteinSpike protein
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: SADS-CoV glycoprotein

SupramoleculeName: SADS-CoV glycoprotein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Swine acute diarrhea syndrome coronavirus
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)

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Macromolecule #1: Spike glycoprotein

MacromoleculeName: Spike glycoprotein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Swine acute diarrhea syndrome coronavirus
Molecular weightTheoretical: 124.780586 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MKLFTVFTLL ASIRVLYGCE SVDFNLFNTI FSTHRGLSNT TSVITGAYPS TNKSDWSCNT RTGHLSGSGF GIGLYVQTPR EQYQYDGSG AGGYTIAVSP IHVTNLTWEL WIHRKWGVNS VVTVRLCRWW QFMSFNSTSH AADAGPTNAF ECLINGSYPT H RNTGYMFG ...String:
MKLFTVFTLL ASIRVLYGCE SVDFNLFNTI FSTHRGLSNT TSVITGAYPS TNKSDWSCNT RTGHLSGSGF GIGLYVQTPR EQYQYDGSG AGGYTIAVSP IHVTNLTWEL WIHRKWGVNS VVTVRLCRWW QFMSFNSTSH AADAGPTNAF ECLINGSYPT H RNTGYMFG VTWYNDLVRI VFPPTVLEMQ LDGLQWERVQ FNSPVNAGHA TRFNVVKDIS TVLVETNSGG SVFRYSYCAD GF VNGLQCK LRLFDIPPGV YSNSEVEYPT ALYTVVHNMS ACPERPDSYC GSNSCPFKRA VFSNCIVNYT TWVNPDQRDF QHL ILSNGK FNPFTECNGL NRIVDGCVPG FVLRVGRGKA VNRTIVTPYL KPYECFGWSW NDNQDSIYDW WIADFVSTGA FVCE SNPEA PKTGVCVTYT VEKVTFQGVL YESNFTFAQY YNLLYVGSQL RYVRILGKVY EVSSCFEASY DVLYRNNQSF GLLYR SFDC NQLHIKSARF VDRLLPSHNG TATVLGCLFN ASYAPNDTMV NCTNPLGDGF CADLLGNVAV RRMTFEKHDT TYVAPV TNE RYTEMPLDHQ LILTEQFLQT TMPKFSVSCE TYICDVSKAC KNLLFRYGGF CQKVEADIRG AGILLDGDVS SLYSTIA AK TSSVVPTTDR FNVSQFFLPK TQSSANKYES RSAIEDLLFS KIETTGPGFY GDYYNCKKNA IQDLTCAQYH NGILVIPP I MDAETLGMYG GIAAASVTLG IFGGQAGMAT WSVAMAGRLN ALGVVQNALV DDVNKLANGF NQLTASVSKL ALTTSSALQ AIQAVVNQNA AQVESLVSGI TENFGAISTN FKVISQRLDK LEADVQMDRL INGRMNVLQL FVTNYKLKIA ELRNTHRYVQ SLINECVYA QSLRNGFCGQ GLHVLSLMQN APSGIMFFHY SLIPNNTITV KTTPGLCESD ELGSKCIVAK DGVLVSANLS Y WQWSPRNL YKPENLTFAN VIAVSRGANY TTLNKTFDIP ELNSTFPIEE EFREYFQNMS SELQVLKNLT ADMSKLNISA EI QLINEIA HNVSNMRVEV EKFQRYVNYV KLEVLFQGPG GGSGGGSGYI PEAPRDGQAY VRKDGEWVLL STFLGWSHPQ FEK

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Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 33 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.3 mg/mL
BufferpH: 7.2
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 49.784 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.83 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 152334

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