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- EMDB-30162: Epstein-Barr virus, icosahedral tegumented capsid reconstruction -

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Basic information

Entry
Database: EMDB / ID: EMD-30162
TitleEpstein-Barr virus, icosahedral tegumented capsid reconstructionEpstein–Barr virus
Map data
Sample
  • Virus: Human gammaherpesvirus 4 (Epstein-Barr virus)
  • Protein or peptide: Small capsomere-interacting protein
  • Protein or peptide: Major capsid protein
  • Protein or peptide: Triplex capsid protein 1
  • Protein or peptide: Triplex capsid protein 2
Function / homology
Function and homology information


T=16 icosahedral viral capsid / viral capsid assembly / viral process / viral capsid / host cell nucleus / structural molecule activity / DNA binding
Similarity search - Function
Gammaherpesvirus capsid / Gammaherpesvirus capsid protein / Herpesvirus capsid protein 2 / Herpesvirus capsid shell protein 1 / Herpesvirus VP23 like capsid protein / Herpesvirus capsid shell protein VP19C / Herpesvirus major capsid protein / Herpesvirus major capsid protein, upper domain superfamily / Herpes virus major capsid protein
Similarity search - Domain/homology
Triplex capsid protein 1 / Major capsid protein / Small capsomere-interacting protein / Triplex capsid protein 2
Similarity search - Component
Biological speciesHHV-4 (Epstein-Barr virus) / Human gammaherpesvirus 4 (Epstein-Barr virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.1 Å
AuthorsLi Z / Yu X
Funding support China, 5 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31900869 China
National Natural Science Foundation of China (NSFC)81702001 China
National Natural Science Foundation of China (NSFC)81830090 China
Ministry of Science and Technology (MoST, China)2016YFA0502101 China
Ministry of Science and Technology (MoST, China)2017YFA0505600 China
CitationJournal: Cell Res / Year: 2020
Title: CryoEM structure of the tegumented capsid of Epstein-Barr virus.
Authors: Zhihai Li / Xiao Zhang / Lili Dong / Jingjing Pang / Miao Xu / Qian Zhong / Mu-Sheng Zeng / Xuekui Yu /
Abstract: Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, ...Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC). Our in situ portal from the tegumented capsid adopts a closed conformation with its channel valve holding the terminal viral DNA and with its crown region firmly engaged by three layers of ring-like dsDNA, which, together with the penton flexibility, effectively alleviates the capsid inner pressure placed on the portal cap. In contrast, the CATCs, through binding to the flexible penton vertices in a stoichiometric manner, accurately increase the inner capsid pressure to facilitate the pressure-driven genome delivery. Together, our results provide important insights into the mechanism by which the EBV capsid, portal, packaged genome and the CATCs coordinately achieve a pressure balance to simultaneously benefit both viral genome retention and ejection.
History
DepositionMar 30, 2020-
Header (metadata) releaseSep 30, 2020-
Map releaseSep 30, 2020-
UpdateOct 14, 2020-
Current statusOct 14, 2020Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.01
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  • Surface view colored by radius
  • Surface level: 0.01
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  • Surface view with fitted model
  • Atomic models: PDB-7bsi
  • Surface level: 0.01
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7bsi
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_30162.png

Downloads & links

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Map

FileDownload / File: emd_30162.map.gz / Format: CCP4 / Size: 4 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.31 Å
Density
Contour LevelBy AUTHOR: 0.01 / Movie #1: 0.01
Minimum - Maximum-0.012542035 - 0.03568149
Average (Standard dev.)0.00227435 (±0.0031766829)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions102410241024
Spacing102410241024
CellA=B=C: 1341.44 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.311.311.31
M x/y/z102410241024
origin x/y/z0.0000.0000.000
length x/y/z1341.4401341.4401341.440
α/β/γ90.00090.00090.000
start NX/NY/NZ212211153
NX/NY/NZ80102186
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS102410241024
D min/max/mean-0.0130.0360.002

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Supplemental data

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Sample components

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Entire : Human gammaherpesvirus 4

EntireName: Human gammaherpesvirus 4 (Epstein-Barr virus)
Components
  • Virus: Human gammaherpesvirus 4 (Epstein-Barr virus)
  • Protein or peptide: Small capsomere-interacting protein
  • Protein or peptide: Major capsid protein
  • Protein or peptide: Triplex capsid protein 1
  • Protein or peptide: Triplex capsid protein 2

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Supramolecule #1: Human gammaherpesvirus 4

SupramoleculeName: Human gammaherpesvirus 4 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 10376 / Sci species name: Human gammaherpesvirus 4 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No

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Macromolecule #1: Small capsomere-interacting protein

MacromoleculeName: Small capsomere-interacting protein / type: protein_or_peptide / ID: 1 / Number of copies: 16 / Enantiomer: LEVO
Source (natural)Organism: HHV-4 (Epstein-Barr virus) / Strain: B95-8
Molecular weightTheoretical: 18.1691 KDa
SequenceString:
MARRLPKPTL QGRLEADFPD SPLLPKFQEL NQNNLPNDVF REAQRSYLVF LTSQFCYEEY VQRTFGVPRR QRAIDKRQRA SVAGAGAHA HLGGSSATPV QQAQAAASAG TGALASSAPS TAVAQSATPS VSSSISSLRA ATSGATAAAS AAAAVDTGSG G GGQPHDTA PRGARKKQ

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Macromolecule #2: Major capsid protein

MacromoleculeName: Major capsid protein / type: protein_or_peptide / ID: 2 / Number of copies: 16 / Enantiomer: LEVO
Source (natural)Organism: HHV-4 (Epstein-Barr virus) / Strain: B95-8
Molecular weightTheoretical: 154.086828 KDa
SequenceString: MASNEGVENR PFPYLTVDAD LLSNLRQSAA EGLFHSFDLL VGKDAREAGI KFEVLLGVYT NAIQYVRFLE TALAVSCVNT EFKDLSRMT DGKIQFRISV PTIAHGDGRR PSKQRTFIVV KNCHKHHIST EMELSMLDLE ILHSIPETPV EYAEYVGAVK T VASALQFG ...String:
MASNEGVENR PFPYLTVDAD LLSNLRQSAA EGLFHSFDLL VGKDAREAGI KFEVLLGVYT NAIQYVRFLE TALAVSCVNT EFKDLSRMT DGKIQFRISV PTIAHGDGRR PSKQRTFIVV KNCHKHHIST EMELSMLDLE ILHSIPETPV EYAEYVGAVK T VASALQFG VDALERGLIN TVLSVKLRHA PPMFILQTLA DPTFTERGFS KTVKSDLIAM FKRHLLEHSF FLDRAENMGS GF SQYVRSR LSEMVAAVSG ESVLKGVSTY TTAKGGEPVG GVFIVTDNVL RQLLTFLGEE ADNQIMGPSS YASFVVRGEN LVT AVSYGR VMRTFEHFMA RIVDSPEKAG STKSDLPAVA AGVEDQPRVP ISAAVIKLGN HAVAVESLQK MYNDTQSPYP LNRR MQYSY YFPVGLFMPN PKYTTSAAIK MLDNPTQQLP VEAWIVNKNN LLLAFNLQNA LKVLCHPRLH TPAHTLNSLN AAPAP RDRR ETYSLQHRRP NHMNVLVIVD EFYDNKYAAP VTDIALKCGL PTEDFLHPSN YDLLRLELHP LYDIYIGRDA GERARH RAV HRLMVGNLPT PLAPAAFQEA RGQQFETATS LAHVVDQAVI ETVQDTAYDT AYPAFFYVVE AMIHGFEEKF VMNVPLV SL CINTYWERSG RLAFVNSFSM IKFICRHLGN NAISKEAYSM YRKIYGELIA LEQALMRLAG SDVVGDESVG QYVCALLD P NLLPPVAYTD IFTHLLTVSD RAPQIIIGNE VYADTLAAPQ FIERVGNMDE MAAQFVALYG YRVNGDHDHD FRLHLGPYV DEGHADVLEK IFYYVFLPTC TNAHMCGLGV DFQHVAQTLA YNGPAFSHHF TRDEDILDNL ENGTLRDLLE ISDLRPTVGM IRDLSASFM TCPTFTRAVR VSVDNDVTQQ LAPNPADKRT EQTVLVNGLV AFAFSERTRA VTQCLFHAIP FHMFYGDPRV A ATMHQDVA TFVMRNPQQR AVEAFNRPEQ LFAEYREWHR SPMGKYAAEC LPSLVSISGM TAMHIKMSPM AYIAQAKLKI HP GVAMTVV RTDEILSENI LFSSRASTSM FIGTPNVSRR EARVDAVTFE VHHEMASIDT GLSYSSTMTP ARVAAITTDM GIH TQDFFS VFPAEAFGNQ QVNDYIKAKV GAQRNGTLLR DPRTYLAGMT NVNGAPGLCH GQQATCEIIV TPVTADVAYF QKSN SPRGR AACVVSCENY NQEVAEGLIY DHSRPDAAYE YRSTVNPWAS QLGSLGDIMY NSSYRQTAVP GLYSPCRAFF NKEEL LRNN RGLYNMVNEY SQRLGGHPAT SNTEVQFVVI AGTDVFLEQP CSFLQEAFPA LSASSRALID EFMSVKQTHA PIHYGH YII EEVAPVRRIL KFGNKVVF

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Macromolecule #3: Triplex capsid protein 1

MacromoleculeName: Triplex capsid protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: HHV-4 (Epstein-Barr virus) / Strain: B95-8
Molecular weightTheoretical: 39.231539 KDa
SequenceString: MKVQGSVDRR RLQRRIAGLL PPPARRLNIS RGSEFTRDVR GLVEEHAQAS SLSAAAVWRA GLLAPGEVAV AGGGSGGGSF SWSGWRPPV FGDFLIHASS FNNAEATGTP LFQFKQSDPF SGVDAVFTPL SLFILMNHGR GVAARVEAGG GLTRMANLLY D SPATLADL ...String:
MKVQGSVDRR RLQRRIAGLL PPPARRLNIS RGSEFTRDVR GLVEEHAQAS SLSAAAVWRA GLLAPGEVAV AGGGSGGGSF SWSGWRPPV FGDFLIHASS FNNAEATGTP LFQFKQSDPF SGVDAVFTPL SLFILMNHGR GVAARVEAGG GLTRMANLLY D SPATLADL VPDFGRLVAD RRFHNFITPV GPLVENIKST YLNKITTVVH GPVVSKAIPR STVKVTVPQE AFVDLDAWLS GG AGGGGGV CFVGGLGLQP CPADARLYVA LTYEEAGPRF TFFQSSRGHC QIMNILRIYY SPSIMHRYAV VQPLHIEELT FGA VACLGT FSATDGWRRS AFNYRGSSLP VVEIDSFYSN VSDWEVIL

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Macromolecule #4: Triplex capsid protein 2

MacromoleculeName: Triplex capsid protein 2 / type: protein_or_peptide / ID: 4 / Number of copies: 10 / Enantiomer: LEVO
Source (natural)Organism: HHV-4 (Epstein-Barr virus) / Strain: B95-8
Molecular weightTheoretical: 33.654039 KDa
SequenceString: MDLKVVVSLS SRLYTDEIAK MQQRIGCILP LASTHGTQNV QGLGLGQVYS LETVPDYVSM YNYLSDCTLA VLDEVSVDSL ILTKIVPGQ TYAIKNKYQP FFQWHGTGSL SVMPPVFGRE HATVKLESND VDIVFPMVLP TPIAEEVLQK ILLFNVYSRV V MQAPGNAD ...String:
MDLKVVVSLS SRLYTDEIAK MQQRIGCILP LASTHGTQNV QGLGLGQVYS LETVPDYVSM YNYLSDCTLA VLDEVSVDSL ILTKIVPGQ TYAIKNKYQP FFQWHGTGSL SVMPPVFGRE HATVKLESND VDIVFPMVLP TPIAEEVLQK ILLFNVYSRV V MQAPGNAD MLDVHMHLGS VSYLGHHYEL ALPEVPGPLG LALLDNLSLY FCIMVTLLPR ASMRLVRGLI RHEHHDLLNL FQ EMVPDEI ARIDLDDLSV ADDLSRMRVM MTYLQSLASL FNLGPRLATA AYSQETLTAT CWLR

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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: 7.5
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: OTHER / Imaging mode: OTHER
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 48.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: RELION (ver. 3.0)
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final 3D classificationSoftware - Name: RELION (ver. 3.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final reconstructionApplied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 32721

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