[English] 日本語
Yorodumi
- EMDB-3111: Insight into the assembly of viruses with vertical single beta-ba... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-3111
TitleInsight into the assembly of viruses with vertical single beta-barrel major capsid proteins
Map datasub-tomogram averaging of five-fold vertices with spike-ON. This has been then gaussian filterd to 15 Ang.
Sample
  • Sample: Haloarcula hispanica icosahedral virus 2 (HHIV-2)
  • Virus: Haloarcula hispanica icosahedral virus 2
Keywordsarchaeal virus / assembly / spike complex-on
Biological speciesHaloarcula hispanica icosahedral virus 2
Methodsubtomogram averaging / cryo EM / Resolution: 38.0 Å
AuthorsGil-Carton D / Jaakkola ST / Charro D / Peralta B / Castano-Diez D / Oksanen HM / Bamford DH / Abrescia NG
CitationJournal: Structure / Year: 2015
Title: Insight into the Assembly of Viruses with Vertical Single β-barrel Major Capsid Proteins.
Authors: David Gil-Carton / Salla T Jaakkola / Diego Charro / Bibiana Peralta / Daniel Castaño-Díez / Hanna M Oksanen / Dennis H Bamford / Nicola G A Abrescia /
Abstract: Archaeal viruses constitute the least explored niche within the virosphere. Structure-based approaches have revealed close relationships between viruses infecting organisms from different domains of ...Archaeal viruses constitute the least explored niche within the virosphere. Structure-based approaches have revealed close relationships between viruses infecting organisms from different domains of life. Here, using biochemical and cryo-electron microscopy techniques, we solved the structure of euryarchaeal, halophilic, internal membrane-containing Haloarcula hispanica icosahedral virus 2 (HHIV-2). We show that the density of the two major capsid proteins (MCPs) recapitulates vertical single β-barrel proteins and that disulfide bridges stabilize the capsid. Below, ordered density is visible close to the membrane and at the five-fold vertices underneath the host-interacting vertex complex underpinning membrane-protein interactions. The HHIV-2 structure exemplifies the division of conserved architectural elements of a virion, such as the capsid, from those that evolve rapidly due to selective environmental pressure such as host-recognizing structures. We propose that in viruses with two vertical single β-barrel MCPs the vesicle is indispensable, and membrane-protein interactions serve as protein-railings for guiding the assembly.
History
DepositionJul 28, 2015-
Header (metadata) releaseAug 26, 2015-
Map releaseSep 9, 2015-
UpdateOct 14, 2015-
Current statusOct 14, 2015Processing site: PDBe / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.1
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by height
  • Surface level: 0.1
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_3111.map.gz / Format: CCP4 / Size: 1001 KB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsub-tomogram averaging of five-fold vertices with spike-ON. This has been then gaussian filterd to 15 Ang.
Voxel sizeX=Y=Z: 7.2 Å
Density
Contour LevelBy AUTHOR: 0.1 / Movie #1: 0.1
Minimum - Maximum-2.31420302 - 2.89222264
Average (Standard dev.)-0.07723363 (±0.65965396)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions646464
Spacing646464
CellA=B=C: 460.8 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z7.27.27.2
M x/y/z646464
origin x/y/z0.0000.0000.000
length x/y/z460.800460.800460.800
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS646464
D min/max/mean-2.3142.892-0.077

-
Supplemental data

-
Sample components

-
Entire : Haloarcula hispanica icosahedral virus 2 (HHIV-2)

EntireName: Haloarcula hispanica icosahedral virus 2 (HHIV-2)
Components
  • Sample: Haloarcula hispanica icosahedral virus 2 (HHIV-2)
  • Virus: Haloarcula hispanica icosahedral virus 2

-
Supramolecule #1000: Haloarcula hispanica icosahedral virus 2 (HHIV-2)

SupramoleculeName: Haloarcula hispanica icosahedral virus 2 (HHIV-2) / type: sample / ID: 1000
Details: While the sample is a virus, the subtomogram averaged map correspond to the components forming the five-fold vertices with the spike complex ON.
Oligomeric state: Icosahedral Virus / Number unique components: 1

-
Supramolecule #1: Haloarcula hispanica icosahedral virus 2

SupramoleculeName: Haloarcula hispanica icosahedral virus 2 / type: virus / ID: 1 / Details: HHIV-2 is a lipid-containing virus / NCBI-ID: 1154689 / Sci species name: Haloarcula hispanica icosahedral virus 2 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No
Host (natural)Organism: Haloarcula hispanica (Halophile) / synonym: ARCHAEA
Virus shellShell ID: 1 / Name: SPIKE COMPLEX-ON

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation stateparticle

-
Sample preparation

Concentration0.9 mg/mL
BufferpH: 7.2
Details: 20 mM Tris-HCl [pH 7.2], 20 mM MgCl2, 10 mM CaCl2, and 0.5 M NaCl
GridDetails: 200-mesh Quantifoil R 3.5/1 holey-carbon grids
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 100 K / Instrument: FEI VITROBOT MARK II / Method: Blot for 3 seconds before plunging

-
Electron microscopy

MicroscopeJEOL 2200FSC
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated magnification: 42147 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2 mm / Nominal defocus max: 6.0 µm / Nominal defocus min: 2.5 µm / Nominal magnification: 30000
Specialist opticsEnergy filter - Name: Omega / Energy filter - Lower energy threshold: 0.0 eV / Energy filter - Upper energy threshold: 30.0 eV
Sample stageSpecimen holder: Ultra-high tilt cryotransfer holder (Model 914 High tilt Tomography Holder, GATAN)
Specimen holder model: GATAN LIQUID NITROGEN / Tilt series - Axis1 - Min angle: -65 ° / Tilt series - Axis1 - Max angle: 65 °
TemperatureMin: 80 K / Max: 103 K / Average: 99 K
Alignment procedureLegacy - Astigmatism: Objective lens astigmatism was corrected at 100,000 times magnification
DateJun 17, 2014
Image recordingCategory: CCD / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k) / Digitization - Sampling interval: 15 µm / Average electron dose: 80 e/Å2
Details: Single-axis tilt series collection under low-dose conditions was automated with SerialEM data acquisition software.
Bits/pixel: 32

-
Image processing

CTF correctionDetails: TOMOCTF method
Final 3D classificationNumber classes: 5
Final reconstructionApplied symmetry - Point group: C5 (5 fold cyclic) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 38.0 Å / Resolution method: OTHER / Software - Name: IMOD, Dynamo / Number subtomograms used: 852
DetailsThe subtomograms were selected using Dynamo with automatic selection of the five-fold vertices. The extracted vertices were then submitted to a multireference alignment procedure with 5 classes.

+
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