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- EMDB-11300: Coxsackievirus B4 strain E2 -

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Basic information

Entry
Database: EMDB / ID: EMD-11300
TitleCoxsackievirus B4 strain E2
Map dataCoxsackievirus B4 strain E2
Sample
  • Virus: Coxsackievirus B4 (strain E2)
    • Protein or peptide: Capsid protein VP1
    • Protein or peptide: Capsid protein VP2
    • Protein or peptide: Capsid protein VP3
    • Protein or peptide: Capsid protein VP4
KeywordsCoxsackievirus B4 / VIRUS
Function / homology
Function and homology information


symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase / channel activity ...symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / DNA replication / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding
Similarity search - Function
Picornavirus coat protein VP4 superfamily / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) ...Picornavirus coat protein VP4 superfamily / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Picornavirus capsid / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biological speciesCoxsackievirus B4 (strain E2)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsFlatt JW / Domanska A
Funding support Finland, 2 items
OrganizationGrant numberCountry
Academy of Finland315950 Finland
Sigrid Juselius Foundation Finland
CitationJournal: Commun Biol / Year: 2021
Title: Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enteroviruses.
Authors: Justin W Flatt / Aušra Domanska / Alma L Seppälä / Sarah J Butcher /
Abstract: Enteroviruses pose a persistent and widespread threat to human physical health, with no specific treatments available. Small molecule capsid binders have the potential to be developed as antivirals ...Enteroviruses pose a persistent and widespread threat to human physical health, with no specific treatments available. Small molecule capsid binders have the potential to be developed as antivirals that prevent virus attachment and entry into host cells. To aid with broad-range drug development, we report here structures of coxsackieviruses B3 and B4 bound to different interprotomer-targeting capsid binders using single-particle cryo-EM. The EM density maps are beyond 3 Å resolution, providing detailed information about interactions in the ligand-binding pocket. Comparative analysis revealed the residues that form a conserved virion-stabilizing network at the interprotomer site, and showed the small molecule properties that allow anchoring in the pocket to inhibit virus disassembly.
History
DepositionJul 3, 2020-
Header (metadata) releaseMar 17, 2021-
Map releaseMar 17, 2021-
UpdateMay 1, 2024-
Current statusMay 1, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.00816
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.00816
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6zms
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6zms
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11300.png

Downloads & links

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Map

FileDownload / File: emd_11300.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCoxsackievirus B4 strain E2
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.24 Å/pix.
x 400 pix.
= 496. Å		1.24 Å/pix.
x 400 pix.
= 496. Å		1.24 Å/pix.
x 400 pix.
= 496. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.24 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.00816 / Movie #1: 0.00816
Minimum - Maximum-0.04550528 - 0.083117016
Average (Standard dev.)0.0009391678 (±0.0053684674)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 496.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.241.241.24
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z496.000496.000496.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.0460.0830.001

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Supplemental data

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Sample components

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Entire : Coxsackievirus B4 (strain E2)

EntireName: Coxsackievirus B4 (strain E2)
Components
  • Virus: Coxsackievirus B4 (strain E2)
    • Protein or peptide: Capsid protein VP1
    • Protein or peptide: Capsid protein VP2
    • Protein or peptide: Capsid protein VP3
    • Protein or peptide: Capsid protein VP4

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Supramolecule #1: Coxsackievirus B4 (strain E2)

SupramoleculeName: Coxsackievirus B4 (strain E2) / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 103905 / Sci species name: Coxsackievirus B4 (strain E2) / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No
Host (natural)Organism: Homo sapiens (human)
Virus shellShell ID: 1 / Name: icosahedral / Diameter: 300.0 Å / T number (triangulation number): 3

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Macromolecule #1: Capsid protein VP1

MacromoleculeName: Capsid protein VP1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Coxsackievirus B4 (strain E2) / Strain: E2
Molecular weightTheoretical: 30.685498 KDa
SequenceString: MGRVADTIAR GPSNSEQIPA LTAVETGHTS QVDPSDTMQT RHVHNYHSRS ESSIENFLCR SACVIYIKYS SAESNNLKRY AEWVINTRQ VAQLRRKMEM FTYIRCDMEL TFVITSHQEM STATNSDVPV QTHQIMYVPP GGPVPTSVND YVWQTSTNPS I FWTEGNAP ...String:
MGRVADTIAR GPSNSEQIPA LTAVETGHTS QVDPSDTMQT RHVHNYHSRS ESSIENFLCR SACVIYIKYS SAESNNLKRY AEWVINTRQ VAQLRRKMEM FTYIRCDMEL TFVITSHQEM STATNSDVPV QTHQIMYVPP GGPVPTSVND YVWQTSTNPS I FWTEGNAP PRMSIPFMSI GNAYTMFYDG WSNFSRDGIY GYNSLNNMGT IYARHVNDSS PGGLTSTIRI YFKPKHVKAY VP RPPRLCQ YKKAKNVNFD VEAVTTERAS LVTT

UniProtKB: Genome polyprotein

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Macromolecule #2: Capsid protein VP2

MacromoleculeName: Capsid protein VP2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Coxsackievirus B4 (strain E2) / Strain: E2
Molecular weightTheoretical: 27.70807 KDa
SequenceString: SDRVRSITLG NSTITTQECA NVVVGYGVWP DYLSDEEATA EDQPTQPDVA TCRFYTLNSV KWEMQSAGWW WKFPDALSEM GLFGQNMQY HYLGRSGYTI HVQCNASKFH QGCLLVVCVP EAEMGCTNAE NAPTYGDLCG GETAKQFEQN AVTGETAVQT A VCNAGMGV ...String:
SDRVRSITLG NSTITTQECA NVVVGYGVWP DYLSDEEATA EDQPTQPDVA TCRFYTLNSV KWEMQSAGWW WKFPDALSEM GLFGQNMQY HYLGRSGYTI HVQCNASKFH QGCLLVVCVP EAEMGCTNAE NAPTYGDLCG GETAKQFEQN AVTGETAVQT A VCNAGMGV GVGNLTIYPH QWINLRTNNS ATIVMPYINS VPMDNMFRHN NFTLMIIPFA PLDYVTGASS YIPITVTVAP MS AEYNGLR LAGHQ

UniProtKB: Genome polyprotein

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Macromolecule #3: Capsid protein VP3

MacromoleculeName: Capsid protein VP3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Coxsackievirus B4 (strain E2) / Strain: E2
Molecular weightTheoretical: 26.44416 KDa
SequenceString: GLPTMLTPGS TQFLTSDDFQ SPSAMPQFDV TPEMNIPGQV RNLMEIAEVD SVVPINNLQA NLKTMEAYRV QVRSTDEMGG QIFGFPLQP GASSVLQRTL LGEILNYYTH WSGSLKLTFV FCGSAMATGK FLLAYSPPGA GAPDSRKNAM LGTHVIWDVG L QSSCVLCV ...String:
GLPTMLTPGS TQFLTSDDFQ SPSAMPQFDV TPEMNIPGQV RNLMEIAEVD SVVPINNLQA NLKTMEAYRV QVRSTDEMGG QIFGFPLQP GASSVLQRTL LGEILNYYTH WSGSLKLTFV FCGSAMATGK FLLAYSPPGA GAPDSRKNAM LGTHVIWDVG L QSSCVLCV PWISQTHYRY VVDDKYTASG FISCWYQTNV IVPAEAQKSC YIMCFVSACN DFSVRMLRDT QFIKQDTFYQ

UniProtKB: Genome polyprotein

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Macromolecule #4: Capsid protein VP4

MacromoleculeName: Capsid protein VP4 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Coxsackievirus B4 (strain E2) / Strain: E2
Molecular weightTheoretical: 7.499235 KDa
SequenceString:
MGAQVSTQKT GAHETSLSAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDV MIKSLPALN

UniProtKB: Genome polyprotein

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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

BufferpH: 7
Component:
ConcentrationFormulaName
10.0 mMC8H18N2O4SHepes
150.0 mMNaclSodium chloride
2.0 mMMgCl2Magnesium chloride
2.0 mMCaCl2Calcium chloride
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS TALOS F200C
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Tecnai F20 / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 40627
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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