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- EMDB-30228: Varicella-zoster virus capsid -

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Basic information

Entry
Database: EMDB / ID: EMD-30228
TitleVaricella-zoster virus capsid
Map data
Sample
  • Virus: Human alphaherpesvirus 3 (Varicella-zoster virus)
    • Protein or peptide: Major capsid protein
    • Protein or peptide: Small capsomere-interacting protein
    • Protein or peptide: Triplex capsid protein 2
    • Protein or peptide: Triplex capsid protein 1
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
Herpesvirus UL35 / Herpesvirus UL35 family / 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
Capsid protein / Major capsid protein / Small capsomere-interacting protein / Capsid protein
Similarity search - Component
Biological speciesHHV-3,Human alphaherpesvirus 3 / Human alphaherpesvirus 3 (Varicella-zoster virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsWang PY / Qi JX / Liu CC / Sun JQ
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)81673358 China
CitationJournal: Nat Commun / Year: 2020
Title: Cryo-EM structure of the varicella-zoster virus A-capsid.
Authors: Junqing Sun / Congcong Liu / Ruchao Peng / Fu-Kun Zhang / Zhou Tong / Sheng Liu / Yi Shi / Zhennan Zhao / Wen-Bo Zeng / George Fu Gao / Hong-Jie Shen / Xiaoming Yang / Minhua Luo / Jianxun Qi / Peiyi Wang /
Abstract: Varicella-zoster virus (VZV), a member of the Alphaherpesvirinae subfamily, causes severe diseases in humans of all ages. The viral capsids play critical roles in herpesvirus infection, making them ...Varicella-zoster virus (VZV), a member of the Alphaherpesvirinae subfamily, causes severe diseases in humans of all ages. The viral capsids play critical roles in herpesvirus infection, making them potential antiviral targets. Here, we present the 3.7-Å-resolution structure of the VZV A-capsid and define the molecular determinants underpinning the assembly of this complicated viral machinery. Overall, the VZV capsid has a similar architecture to that of other known herpesviruses. The major capsid protein (MCP) assembles into pentons and hexons, forming extensive intra- and inter-capsomer interaction networks that are further secured by the small capsid protein (SCP) and the heterotriplex. The structure reveals a pocket beneath the floor of MCP that could potentially be targeted by antiviral inhibitors. In addition, we identified two alphaherpesvirus-specific structural features in SCP and Tri1 proteins. These observations highlight the divergence of different herpesviruses and provide an important basis for developing antiviral drugs.
History
DepositionApr 13, 2020-
Header (metadata) releaseSep 23, 2020-
Map releaseSep 23, 2020-
UpdateOct 7, 2020-
Current statusOct 7, 2020Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.01
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.01
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  • Surface view with fitted model
  • Atomic models: PDB-7bw6
  • Surface level: 0.01
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7bw6
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_30228.png

Downloads & links

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Map

FileDownload / File: emd_30228.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.41 Å
Density
Contour LevelBy AUTHOR: 0.01 / Movie #1: 0.01
Minimum - Maximum-0.053119987 - 0.10360403
Average (Standard dev.)0.0010633004 (±0.0073867715)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 564.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.411.411.41
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z564.000564.000564.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ400400400
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.0530.1040.001

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Supplemental data

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Additional map: #1

Fileemd_30228_additional.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human alphaherpesvirus 3

EntireName: Human alphaherpesvirus 3 (Varicella-zoster virus)
Components
  • Virus: Human alphaherpesvirus 3 (Varicella-zoster virus)
    • Protein or peptide: Major capsid protein
    • Protein or peptide: Small capsomere-interacting protein
    • Protein or peptide: Triplex capsid protein 2
    • Protein or peptide: Triplex capsid protein 1

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Supramolecule #1: Human alphaherpesvirus 3

SupramoleculeName: Human alphaherpesvirus 3 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10335 / Sci species name: Human alphaherpesvirus 3 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes

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Macromolecule #1: Major capsid protein

MacromoleculeName: Major capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 16 / Enantiomer: LEVO
Source (natural)Organism: HHV-3,Human alphaherpesvirus 3
Molecular weightTheoretical: 155.145359 KDa
SequenceString: MTTVSCPANV ITTTESDRIA GLFNIPAGII PTGNVLSTIE VCAHRCIFDF FKQIRSDDNS LYSAQFDILL GTYCNTLNFV RFLELGLSV ACICTKFPEL AYVRDGVIQF EVQQPMIARD GPHPVDQPVH NYMVKRIHKR SLSAAFAIAS EALSLLSNTY V DGTEIDSS ...String:
MTTVSCPANV ITTTESDRIA GLFNIPAGII PTGNVLSTIE VCAHRCIFDF FKQIRSDDNS LYSAQFDILL GTYCNTLNFV RFLELGLSV ACICTKFPEL AYVRDGVIQF EVQQPMIARD GPHPVDQPVH NYMVKRIHKR SLSAAFAIAS EALSLLSNTY V DGTEIDSS LRIRAIQQMA RNLRTVLDSF ERGTADQLLG VLLEKAPPLS LLSPINKFQP EGHLNRVARA ALLSDLKRRV CA DMFFMTR HAREPRLISA YLSDMVSCTQ PSVMVSRITH TNTRGRQVDG VLVTTATLKR QLLQGILQID DTAADVPVTY GEM VLQGTN LVTALVMGKA VRGMDDVARH LLDITDPNTL NIPSIPPQSN SDSTTAGLPV NARVPADLVI VGDKLVFLEA LERR VYQAT RVAYPLIGNI DITFIMPMGV FQANSMDRYT RHAGDFSTVS EQDPRQFPPQ GIFFYNKDGI LTQLTLRDAM GTICH SSLL DVEATLVALR QQHLDRQCYF GVYVAEGTED TLDVQMGRFM ETWADMMPHH PHWVNEHLTI LQFIAPSNPR LRFELN PAF DFFVAPGDVD LPGPQRPPEA MPTVNATLRI INGNIPVPLC PISFRDCRGT QLGLGRHTMT PATIKAVKDT FEDRAYP TI FYMLEAVIHG NERNFCALLR LLTQCIRGYW EQSHRVAFVN NFHMLMYITT YLGNGELPEV CINIYRDLLQ HVRALRQT I TDFTIQGEGH NGETSEALNN ILTDDTFIAP ILWDCDALIY RDEAARDRLP AIRVSGRNGY QALHFVDMAG HNFQRRDNV LIHGRPVRGD TGQGIPITPH HDREWGILSK IYYYIVIPAF SRGSCCTMGV RYDRLYPALQ AVIVPEIPAD EEAPTTPEDP RHPLHAHQL VPNSLNVYFH NAHLTVDGDA LLTLQELMGD MAERTTAILV SSAPDAGAAT ATTRNMRIYD GALYHGLIMM A YQAYDETI ATGTFFYPVP VNPLFACPEH LASLRGMTNA RRVLAKMVPP IPPFLGANHH ATIRQPVAYH VTHSKSDFNT LT YSLLGGY FKFTPISLTH QLRTGFHPGI AFTVVRQDRF ATEQLLYAER ASESYFVGQI QVHHHDAIGG VNFTLTQPRA HVD LGVGYT AVCATAALRC PLTDMGNTAQ NLFFSRGGVP MLHDNVTESL RRITASGGRL NPTEPLPIFG GLRPATSAGI ARGQ ASVCE FVAMPVSTDL QYFRTACNPR GRASGMLYMG DRDADIEAIM FDHTQSDVAY TDRATLNPWA SQKHSYGDRL YNGTY NLTG ASPIYSPCFK FFTPAEVNTN CNTLDRLLME AKAVASQSST DTEYQFKRPP GSTEMTQDPC GLFQEAYPPL CSSDAA MLR TAHAGETGAD EVHLAQYLIR DASPLRGCLP LPR

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Macromolecule #2: Small capsomere-interacting protein

MacromoleculeName: Small capsomere-interacting protein / type: protein_or_peptide / ID: 2 / Number of copies: 15 / Enantiomer: LEVO
Source (natural)Organism: HHV-3,Human alphaherpesvirus 3
Molecular weightTheoretical: 24.440119 KDa
SequenceString: MTQPASSRVV FDPSNPTTFS VEAIAAYTPV ALIRLLNASG PLQPGHRVDI ADARSIYTVG AAASAARARA NHNANTIRRT AMFAETDPM TWLRPTVGLK RTFNPRIIRP QPPNPSMSLG ISGPTILPQK TQSADQSALQ QPAALAFSGS SPQHPPPQTT S ASVGQQQH ...String:
MTQPASSRVV FDPSNPTTFS VEAIAAYTPV ALIRLLNASG PLQPGHRVDI ADARSIYTVG AAASAARARA NHNANTIRRT AMFAETDPM TWLRPTVGLK RTFNPRIIRP QPPNPSMSLG ISGPTILPQK TQSADQSALQ QPAALAFSGS SPQHPPPQTT S ASVGQQQH VVSGSSGQQP QQGAQSSTVQ PTTGSPPAAQ GVPQSTPPPT QNTPQGGKGQ TLSHTGQSGN ASRSRRV

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Macromolecule #3: Triplex capsid protein 2

MacromoleculeName: Triplex capsid protein 2 / type: protein_or_peptide / ID: 3 / Number of copies: 10 / Enantiomer: LEVO
Source (natural)Organism: HHV-3,Human alphaherpesvirus 3
Molecular weightTheoretical: 34.421914 KDa
SequenceString: MAMPFEIEVL LPGELSPAET SALQKCEGKI ITFSTLRHRA SLVDIALSSY YINGAPPDTL SLLEAYRMRF AAVITRVIPG KLLAHAIGV GTPTPGLFIQ NTSPVDLCNG DYICLLPPVF GSADSIRLDS VGLEIVFPLT IPQTLMREII AKVVARAVER T AAGAQILP ...String:
MAMPFEIEVL LPGELSPAET SALQKCEGKI ITFSTLRHRA SLVDIALSSY YINGAPPDTL SLLEAYRMRF AAVITRVIPG KLLAHAIGV GTPTPGLFIQ NTSPVDLCNG DYICLLPPVF GSADSIRLDS VGLEIVFPLT IPQTLMREII AKVVARAVER T AAGAQILP HEVLRGADVI CYNGRRYELE TNLQHRDGSD AAIRTLVLNL MFSINEGCLL LLALIPTLLV QGAHDGYVNL LI QTANCVR ETGQLINIPP MPRIQDGHRR FPIYETISSW ISTSSRLGDT LGTRAILRVC VFDGPSTVHP GDRTAVIQV

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Macromolecule #4: Triplex capsid protein 1

MacromoleculeName: Triplex capsid protein 1 / type: protein_or_peptide / ID: 4 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: HHV-3,Human alphaherpesvirus 3
Molecular weightTheoretical: 54.02818 KDa
SequenceString: MGSQPTNSHF TLNEQTLCGT NISLLGNNRF IQIGNGLHMT YAPGFFGNWS RDLTIGPRFG GLNKQPIHVP PKRTETASIQ VTPRSIVIN RMNNIQINPT SIGNPQVTIR LPLNNFKSTT QLIQQVSLTD FFRPDIEHAG SIVLILRHPS DMIGEANTLT Q AGRDPDVL ...String:
MGSQPTNSHF TLNEQTLCGT NISLLGNNRF IQIGNGLHMT YAPGFFGNWS RDLTIGPRFG GLNKQPIHVP PKRTETASIQ VTPRSIVIN RMNNIQINPT SIGNPQVTIR LPLNNFKSTT QLIQQVSLTD FFRPDIEHAG SIVLILRHPS DMIGEANTLT Q AGRDPDVL LEGLRNLFNA CTAPWTVGEG GGLRAYVTSL SFIAACRAEE YTDKQAADAN RTAIVSAYGC SRMETRLIRF SE CLRAMVQ CHVFPHRFIS FFGSLLEYTI QDNLCNITAV AKGPQEAART DKTSTRRVTA NIPACVFWDV DKDLHLSADG LKH VFLVFV YTQRRQREGV RLHLALSQLN EQCFGRGIGF LLGRIRAENA AWGTEGVANT HQPYNTRALP LVQLSNDPTS PRCS IGEIT GVNWNLARQR LYQWTGDFRG LPTQLSCMYA AYTLIGTIPS ESVRYTRRME RFGGYNVPTI WLEGVVWGGT NTWNE CYY

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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

Concentration0.5 mg/mL
BufferpH: 7.4
GridModel: Homemade / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: LACEY / Support film - Film thickness: 3.0 nm / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 2 seconds before plunging.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Calibrated defocus max: 5.116 µm / Calibrated defocus min: 0.3863 µm / Calibrated magnification: 59000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 59000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
TemperatureMin: 81.0 K / Max: 93.0 K
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number real images: 26979 / Average electron dose: 40.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 94640
Details: Images were low-pass to 15 angstrom to facilitated particle picking.
CTF correctionSoftware - Name: CTFFIND (ver. 4.1)
Software - details: minimum defocus 0.5um,maximnum defocous 5um
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0.8)
Final 3D classificationNumber classes: 5 / Avg.num./class: 505632 / Software - Name: RELION (ver. 3.0.8)
Software - details: local angular search range 3,sampling interval:0.5degree, +-4 pixel offset search.
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0.8)
Final reconstructionNumber classes used: 5 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0.8) / Number images used: 311236
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

5zz8

chain_id: 1, residue_range: 74-482

5zz8

chain_id: 2, residue_range: 8-316

5zz8

chain_id: A, residue_range: 19-1393

5zz8

chain_id: b, residue_range: 8-107
RefinementSpace: REAL
Output model

PDB-7bw6:
Varicella-zoster virus capsid

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