[English] 日本語
Yorodumi
- EMDB-21504: Structures of Capsid and Capsid-Associated Tegument Complex insid... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-21504
TitleStructures of Capsid and Capsid-Associated Tegument Complex inside the Epstein-Barr Virus
Map dataI3 capsid reconstruction for EBV
Sample
  • Virus: Human herpesvirus 4 strain B95-8 (Epstein-Barr virus (strain B95-8))
    • Protein or peptide: Major capsid protein
    • Protein or peptide: Small capsomere-interacting protein
    • Protein or peptide: Triplex capsid protein 1
    • Protein or peptide: Triplex capsid protein 2
Keywordsgamma-herpesvirus / EBV / CATC / Structural plasticity / VIRUS
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 speciesEpstein-Barr virus (strain B95-8) (Epstein-Barr virus (strain B95-8)) / Human herpesvirus 4 strain B95-8 (Epstein-Barr virus (strain B95-8))
Methodsingle particle reconstruction / cryo EM / Resolution: 5.5 Å
AuthorsLiu W / Cui YX
Funding support United States, 4 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)DE028583, DE025567 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI094386 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1S10RR23057, 1S10OD018111, and 1U24GM116792 United States
National Science Foundation (NSF, United States)DBI-1338135 and DMR-1548924 United States
CitationJournal: Nat Microbiol / Year: 2020
Title: Structures of capsid and capsid-associated tegument complex inside the Epstein-Barr virus.
Authors: Wei Liu / Yanxiang Cui / Caiyan Wang / Zihang Li / Danyang Gong / Xinghong Dai / Guo-Qiang Bi / Ren Sun / Z Hong Zhou /
Abstract: As the first discovered human cancer virus, Epstein-Barr virus (EBV) causes Burkitt's lymphoma and nasopharyngeal carcinoma. Isolating virions for determining high-resolution structures has been ...As the first discovered human cancer virus, Epstein-Barr virus (EBV) causes Burkitt's lymphoma and nasopharyngeal carcinoma. Isolating virions for determining high-resolution structures has been hindered by latency-a hallmark of EBV infection-and atomic structures are thus available only for recombinantly expressed EBV proteins. In the present study, by symmetry relaxation and subparticle reconstruction, we have determined near-atomic-resolution structures of the EBV capsid with an asymmetrically attached DNA-translocating portal and capsid-associated tegument complexes from cryogenic electron microscopy images of just 2,048 EBV virions obtained by chemical induction. The resulting atomic models reveal structural plasticity among the 20 conformers of the major capsid protein, 2 conformers of the small capsid protein (SCP), 4 conformers of the triplex monomer proteins and 2 conformers of the triplex dimer proteins. Plasticity reaches the greatest level at the capsid-tegument interfaces involving SCP and capsid-associated tegument complexes (CATC): SCPs crown pentons/hexons and mediate tegument protein binding, and CATCs bind and rotate all five periportal triplexes, but notably only about one peri-penton triplex. These results offer insights into the EBV capsid assembly and a mechanism for recruiting cell-regulating factors into the tegument compartment as 'cargoes', and should inform future anti-EBV strategies.
History
DepositionMar 3, 2020-
Header (metadata) releaseApr 15, 2020-
Map releaseJul 15, 2020-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.02
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.02
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-6w19
  • Surface level: 0.02
  • Imaged by UCSF Chimera
  • Download
  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6w19
  • Imaged by Jmol
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21504.png

Downloads & links

-
Map

FileDownload / File: emd_21504.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationI3 capsid reconstruction for EBV
Voxel sizeX=Y=Z: 2.71 Å
Density
Contour LevelBy AUTHOR: 0.02 / Movie #1: 0.02
Minimum - Maximum-0.015800403 - 0.067396045
Average (Standard dev.)0.006506964 (±0.0071736593)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-256-256-256
Dimensions512512512
Spacing512512512
CellA=B=C: 1387.52 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z2.712.712.71
M x/y/z512512512
origin x/y/z0.0000.0000.000
length x/y/z1387.5201387.5201387.520
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ250250250
MAP C/R/S123
start NC/NR/NS-256-256-256
NC/NR/NS512512512
D min/max/mean-0.0160.0670.007

-
Supplemental data

-
Sample components

-
Entire : Human herpesvirus 4 strain B95-8

EntireName: Human herpesvirus 4 strain B95-8 (Epstein-Barr virus (strain B95-8))
Components
  • Virus: Human herpesvirus 4 strain B95-8 (Epstein-Barr virus (strain B95-8))
    • Protein or peptide: Major capsid protein
    • Protein or peptide: Small capsomere-interacting protein
    • Protein or peptide: Triplex capsid protein 1
    • Protein or peptide: Triplex capsid protein 2

-
Supramolecule #1: Human herpesvirus 4 strain B95-8

SupramoleculeName: Human herpesvirus 4 strain B95-8 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10377 / Sci species name: Human herpesvirus 4 strain B95-8 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No

-
Macromolecule #1: Major capsid protein

MacromoleculeName: Major capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 16 / Enantiomer: LEVO
Source (natural)Organism: Epstein-Barr virus (strain B95-8) (Epstein-Barr virus (strain B95-8))
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

UniProtKB: Major capsid protein

-
Macromolecule #2: Small capsomere-interacting protein

MacromoleculeName: Small capsomere-interacting protein / type: protein_or_peptide / ID: 2 / Number of copies: 16 / Enantiomer: LEVO
Source (natural)Organism: Epstein-Barr virus (strain B95-8) (Epstein-Barr virus (strain B95-8))
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

UniProtKB: Small capsomere-interacting protein

-
Macromolecule #3: Triplex capsid protein 1

MacromoleculeName: Triplex capsid protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Epstein-Barr virus (strain B95-8) (Epstein-Barr virus (strain B95-8))
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

UniProtKB: Triplex capsid protein 1

-
Macromolecule #4: Triplex capsid protein 2

MacromoleculeName: Triplex capsid protein 2 / type: protein_or_peptide / ID: 4 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Epstein-Barr virus (strain B95-8) (Epstein-Barr virus (strain B95-8))
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

UniProtKB: Triplex capsid protein 2

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4 / Details: PBS buffer, pH 7.4
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 101.325 kPa
VitrificationCryogen name: ETHANE / Instrument: HOMEMADE PLUNGER / Details: The grids were manually plunged into the ethane..

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated defocus max: 4.0 µm / Calibrated defocus min: 0.8 µm / Calibrated magnification: 105000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Number real images: 1833 / Average electron dose: 28.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Particle selectionNumber selected: 2801
Startup modelType of model: OTHER
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
Final reconstructionResolution.type: BY AUTHOR / Resolution: 5.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 2048

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more