[English] 日本語
Yorodumi
- EMDB-4014: Structure of deformed wing virus, a honeybee pathogen -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-4014
TitleStructure of deformed wing virus, a honeybee pathogen
Map data
Sample
  • Virus: Deformed wing virus
    • Protein or peptide: VP1
    • Protein or peptide: VP2
    • Protein or peptide: VP3
    • Ligand: URIDINE-5'-MONOPHOSPHATE
KeywordsDeformed wing virus / Picornavirales / Iflaviridae / Iflavirus / viral protein
Function / homology
Function and homology information


host cell membrane / viral capsid / host cell cytoplasm / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / RNA helicase / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity ...host cell membrane / viral capsid / host cell cytoplasm / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / RNA helicase / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / structural molecule activity / proteolysis / RNA binding / ATP binding / membrane / cytoplasm
Similarity search - Function
Dicistrovirus, capsid-polyprotein, C-terminal / CRPV capsid protein like / 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 ...Dicistrovirus, capsid-polyprotein, C-terminal / CRPV capsid protein like / 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. / 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
Genome polyprotein / Genome polyprotein / Genome polyprotein / Genome polyprotein
Similarity search - Component
Biological speciesDeformed wing virus / Apis mellifera (honey bee)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsSkubnik K / Novacek J
Funding support1 items
OrganizationGrant numberCountry
European Research Council355855
CitationJournal: Proc Natl Acad Sci U S A / Year: 2017
Title: Structure of deformed wing virus, a major honey bee pathogen.
Authors: Karel Škubník / Jiří Nováček / Tibor Füzik / Antonín Přidal / Robert J Paxton / Pavel Plevka /
Abstract: The worldwide population of western honey bees () is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) ...The worldwide population of western honey bees () is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) from the family , together with its vector, the mite , is likely the major threat to the world's honey bees. However, lack of knowledge of the atomic structures of iflaviruses has hindered the development of effective treatments against them. Here, we present the virion structures of DWV determined to a resolution of 3.1 Å using cryo-electron microscopy and 3.8 Å by X-ray crystallography. The C-terminal extension of capsid protein VP3 folds into a globular protruding (P) domain, exposed on the virion surface. The P domain contains an Asp-His-Ser catalytic triad that is, together with five residues that are spatially close, conserved among iflaviruses. These residues may participate in receptor binding or provide the protease, lipase, or esterase activity required for entry of the virus into a host cell. Furthermore, nucleotides of the DWV RNA genome interact with VP3 subunits. The capsid protein residues involved in the RNA binding are conserved among honey bee iflaviruses, suggesting a putative role of the genome in stabilizing the virion or facilitating capsid assembly. Identifying the RNA-binding and putative catalytic sites within the DWV virion structure enables future analyses of how DWV and other iflaviruses infect insect cells and also opens up possibilities for the development of antiviral treatments.
History
DepositionJun 8, 2016-
Header (metadata) releaseAug 31, 2016-
Map releaseMar 29, 2017-
UpdateMay 15, 2024-
Current statusMay 15, 2024Processing site: PDBe / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.09
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.09
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-5l8q
  • Surface level: 0.09
  • Imaged by UCSF Chimera
  • Download
  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-5l8q
  • Imaged by Jmol
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4014.png

Downloads & links

-
Map

FileDownload / File: emd_4014.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 512 pix.
= 542.208 Å		1.06 Å/pix.
x 512 pix.
= 542.208 Å		1.06 Å/pix.
x 512 pix.
= 542.208 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.059 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.09 / Movie #1: 0.09
Minimum - Maximum-0.6789989 - 0.9588455
Average (Standard dev.)0.0022389216 (±0.040165383)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-256-256-256
Dimensions512512512
Spacing512512512
CellA=B=C: 542.208 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0591.0591.059
M x/y/z512512512
origin x/y/z0.0000.0000.000
length x/y/z542.208542.208542.208
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS-256-256-256
NC/NR/NS512512512
D min/max/mean-0.6790.9590.002

-
Supplemental data

-
Sample components

-
Entire : Deformed wing virus

EntireName: Deformed wing virus
Components
  • Virus: Deformed wing virus
    • Protein or peptide: VP1
    • Protein or peptide: VP2
    • Protein or peptide: VP3
    • Ligand: URIDINE-5'-MONOPHOSPHATE

-
Supramolecule #1: Deformed wing virus

SupramoleculeName: Deformed wing virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Virus was purified from honeybee pupae / NCBI-ID: 198112 / Sci species name: Deformed wing virus / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No
Host (natural)Organism: Apis mellifera (honey bee)
Virus shellShell ID: 1 / Diameter: 390.0 Å / T number (triangulation number): 3

-
Macromolecule #1: VP1

MacromoleculeName: VP1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Deformed wing virus
Molecular weightTheoretical: 28.679273 KDa
SequenceString: GEESRNTTVL DTTTTLQSSG FGRAFFGEAF NDLKTLMRRY QLYGQLLLSV TTDKDIDHCM FTFPCLPQGL ALDIGSAGSP HEIFNRCRD GIIPLIASGY RFYRGDLRYK IVFPSNVNSN IWVQHRPDRR LEGWSAAKIV NCDAVSTGQG VYNHGYASHI Q ITRVNNVI ...String:
GEESRNTTVL DTTTTLQSSG FGRAFFGEAF NDLKTLMRRY QLYGQLLLSV TTDKDIDHCM FTFPCLPQGL ALDIGSAGSP HEIFNRCRD GIIPLIASGY RFYRGDLRYK IVFPSNVNSN IWVQHRPDRR LEGWSAAKIV NCDAVSTGQG VYNHGYASHI Q ITRVNNVI ELEVPFYNAT CYNYLQAFNA SSAASSYAVS LGEISVGFQA TSDDIASIVN KPVTIYYSIG DGMQFSQWVG YQ PMMILDQ LPAPVVRAVP E

UniProtKB: Genome polyprotein

-
Macromolecule #2: VP2

MacromoleculeName: VP2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Deformed wing virus
Molecular weightTheoretical: 28.3609 KDa
SequenceString: MDNPNPGPDG EGEVELEKDS NVVLTTQRDP STSIPAPVSV KWSRWTSNDV VDDYATITSR WYQIAEFVWS KDDPFDKELA RLILPRALL SSIEANSDAI CDVPNTIPFK VHAYWRGDME VRVQINSNKF QVGQLQATWY YSDHENLNIS SKRSVYGFSQ M DHALISAS ...String:
MDNPNPGPDG EGEVELEKDS NVVLTTQRDP STSIPAPVSV KWSRWTSNDV VDDYATITSR WYQIAEFVWS KDDPFDKELA RLILPRALL SSIEANSDAI CDVPNTIPFK VHAYWRGDME VRVQINSNKF QVGQLQATWY YSDHENLNIS SKRSVYGFSQ M DHALISAS ASNEAKLVIP FKHVYPFLPT RIVPDWTTGI LDMGALNIRV IAPLRMSATG PTTCNVVVFI KLNNSEFTGT SS GKFYASQ IRAKPE

UniProtKB: Genome polyprotein

-
Macromolecule #3: VP3

MacromoleculeName: VP3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Deformed wing virus
Molecular weightTheoretical: 46.697582 KDa
SequenceString: DNPSYQQSPR HFVPTGMHSL ALGTNLVEPL HALRLDAAGT TQHPVGCAPD EDMTVSSIAS RYGLIRRVQW KKDHAKGSLL LQLDADPFV EQRIEGTNPI SLYWFAPVGV VSSMFMQWRG SLEYRFDIIA SQFHTGRLIV GYVPGLTASL QLQMDYMKLK S SSYVVFDL ...String:
DNPSYQQSPR HFVPTGMHSL ALGTNLVEPL HALRLDAAGT TQHPVGCAPD EDMTVSSIAS RYGLIRRVQW KKDHAKGSLL LQLDADPFV EQRIEGTNPI SLYWFAPVGV VSSMFMQWRG SLEYRFDIIA SQFHTGRLIV GYVPGLTASL QLQMDYMKLK S SSYVVFDL QESNSFTFEV PYVSYRPWWV RKYGGNYLPS STDAPSTLFM YVQVPLIPME AVSDTIDINV YVRGGSSFEV CV PVQPSLG LNWNTDFILR NDEEYRAKTG YAPYYAGVWH SFNNSNSLVF RWGSASDQIA QWPTISVPRG ELAFLRIKDG KQA AVGTQP WRTMVVWPSG HGYNIGIPTY NAERARQLAQ HLYGGGSLTD EKAKQLFVPA NQQGPGKVSN GNPVWEVMRA PLAT QRAHI QDFEFIEAIP E

UniProtKB: Genome polyprotein

-
Macromolecule #4: URIDINE-5'-MONOPHOSPHATE

MacromoleculeName: URIDINE-5'-MONOPHOSPHATE / type: ligand / ID: 4 / Number of copies: 1 / Formula: U
Source (natural)Organism: Apis mellifera (honey bee)
Molecular weightTheoretical: 324.181 Da
Chemical component information

ChemComp-U:
URIDINE-5'-MONOPHOSPHATE

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration2.5 mg/mL
BufferpH: 7.4
Details: Dulbeccos Phosphate Buffered Saline D8537 sigma aldrich
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. / Pretreatment - Atmosphere: NITROGEN / Pretreatment - Pressure: 0.007 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Digitization - Frames/image: 2-7 / Number grids imaged: 1 / Number real images: 26 / Average exposure time: 1.0 sec. / Average electron dose: 15.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Calibrated magnification: 74235 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 75000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Particle selectionNumber selected: 141860
Startup modelType of model: OTHER
Details: Model obtained by crystallography with resolution 7.5
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: I (icosahedral) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.4) / Software - details: relion_refine_mpi / Number images used: 26540
Initial angle assignmentType: OTHER
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 1.4) / Software - details: relion_refine_mpi / Details: Relion 3D auto refinement
Final 3D classificationNumber classes: 5 / Avg.num./class: 12000 / Software - Name: RELION (ver. 1.4) / Software - details: relion_refine_mpi
Details: Relion 3D classfication - reclassification after initial 3D refinement
FSC plot (resolution estimation)

-
Atomic model buiding 1

RefinementSpace: REAL / Protocol: OTHER / Target criteria: R-factor
Output model

PDB-5l8q:
Structure of deformed wing virus, a honeybee pathogen

+
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