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- EMDB-6636: The novel asymmetric entry intermediate of a picornavirus capture... -

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Basic information

Entry
Database: EMDB / ID: EMD-6636
TitleThe novel asymmetric entry intermediate of a picornavirus captured with nanodiscs
Map dataIcosahedral reconstruction of CVB3 A-particle
Sample
  • Sample: Locally-stimulated A-particle of CVB3
  • Virus: Human coxsackievirus B3
KeywordsPicornavirus / entry intermediate
Biological speciesHuman coxsackievirus B3
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsShingler KL / Lee H / Organtini LJ / Ashley RE / Subramanian S / Makhov AM / Conway JF / Hafenstein S
CitationJournal: Sci Adv / Year: 2016
Title: The novel asymmetric entry intermediate of a picornavirus captured with nanodiscs.
Authors: Hyunwook Lee / Kristin L Shingler / Lindsey J Organtini / Robert E Ashley / Alexander M Makhov / James F Conway / Susan Hafenstein /
Abstract: Many nonenveloped viruses engage host receptors that initiate capsid conformational changes necessary for genome release. Structural studies on the mechanisms of picornavirus entry have relied on in ...Many nonenveloped viruses engage host receptors that initiate capsid conformational changes necessary for genome release. Structural studies on the mechanisms of picornavirus entry have relied on in vitro approaches of virus incubated at high temperatures or with excess receptor molecules to trigger the entry intermediate or A-particle. We have induced the coxsackievirus B3 entry intermediate by triggering the virus with full-length receptors embedded in lipid bilayer nanodiscs. These asymmetrically formed A-particles were reconstructed using cryo-electron microscopy and a direct electron detector. These first high-resolution structures of a picornavirus entry intermediate captured at a membrane with and without imposing icosahedral symmetry (3.9 and 7.8 Å, respectively) revealed a novel A-particle that is markedly different from the classical A-particles. The asymmetric receptor binding triggers minimal global capsid expansion but marked local conformational changes at the site of receptor interaction. In addition, viral proteins extrude from the capsid only at the site of extensive protein remodeling adjacent to the nanodisc. Thus, the binding of the receptor triggers formation of a unique site in preparation for genome release.
History
DepositionApr 20, 2016-
Header (metadata) releaseJul 13, 2016-
Map releaseSep 14, 2016-
UpdateSep 14, 2016-
Current statusSep 14, 2016Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 2
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 2
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_6636.png

Downloads & links

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Map

FileDownload / File: emd_6636.map.gz / Format: CCP4 / Size: 238.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationIcosahedral reconstruction of CVB3 A-particle
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.37 Å/pix.
x 400 pix.
= 548. Å		1.37 Å/pix.
x 400 pix.
= 548. Å		1.37 Å/pix.
x 400 pix.
= 548. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.37 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 2.0 / Movie #1: 2
Minimum - Maximum-1.53407359 - 6.18506145
Average (Standard dev.)0.0 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-200-200-200
Dimensions400400400
Spacing400400400
CellA=B=C: 548.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.371.371.37
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z548.000548.000548.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS-200-200-200
NC/NR/NS400400400
D min/max/mean-1.5346.1850.000

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Supplemental data

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Sample components

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Entire : Locally-stimulated A-particle of CVB3

EntireName: Locally-stimulated A-particle of CVB3
Components
  • Sample: Locally-stimulated A-particle of CVB3
  • Virus: Human coxsackievirus B3

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Supramolecule #1000: Locally-stimulated A-particle of CVB3

SupramoleculeName: Locally-stimulated A-particle of CVB3 / type: sample / ID: 1000 / Number unique components: 1

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Supramolecule #1: Human coxsackievirus B3

SupramoleculeName: Human coxsackievirus B3 / type: virus / ID: 1
Details: CAR-nanodisc was incubated with the virus sample at 37 degrees Celsius for 30 minutes.
NCBI-ID: 12072 / Sci species name: Human coxsackievirus B3 / Sci species strain: 28 / Database: NCBI / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No
Host (natural)Organism: Homo sapiens (human) / synonym: VERTEBRATES
Virus shellShell ID: 1 / Name: VP1-4 / Diameter: 300 Å / T number (triangulation number): 1

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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

Concentration1.0 mg/mL
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 102 K / Instrument: GATAN CRYOPLUNGE 3

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Electron microscopy

MicroscopeFEI POLARA 300
DateNov 21, 2014
Image recordingCategory: CCD / Film or detector model: FEI FALCON II (4k x 4k) / Number real images: 9685
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.0 mm / Nominal defocus max: 5.875 µm / Nominal defocus min: 1.362 µm
Sample stageSpecimen holder model: SIDE ENTRY, EUCENTRIC
Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company

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Image processing

CTF correctionDetails: Each particle
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: OTHER / Software - Name: RELION / Number images used: 57203

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Atomic model buiding 1

Initial modelPDB ID:

1cov


Chain - #0 - Chain ID: 1 / Chain - #1 - Chain ID: 2 / Chain - #2 - Chain ID: 3 / Chain - #3 - Chain ID: 4
SoftwareName: Phenix
RefinementSpace: REAL / Protocol: FLEXIBLE FIT

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