[English] 日本語
Yorodumi
- EMDB-5467: 4.2 Angstrom Cryo-EM structure of Ad5F35 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-5467
Title4.2 Angstrom Cryo-EM structure of Ad5F35
Map data4.2 Angstrom Cryo-EM reconstruction of Ad5F35
Sample
  • Sample: Ad5F35--human adenovirus type 5 (Ad5) capsid pseudo-typed with an Ad35 fiber
  • Virus: Human adenovirus 5
Keywordshuman adenovirus / fiber / cryo-EM / near-atomic resolution
Biological speciesHuman adenovirus 5
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsCao C / Dong X / Wu X / Ji G / Cheng L / Liu H
CitationJournal: J Virol / Year: 2012
Title: Conserved fiber-penton base interaction revealed by nearly atomic resolution cryo-electron microscopy of the structure of adenovirus provides insight into receptor interaction.
Authors: Changchun Cao / Xiaoyan Dong / Xiaobing Wu / Boyun Wen / Gang Ji / Lingpeng Cheng / Hongrong Liu /
Abstract: Adenovirus (Ad) cell attachment is initiated by the attachment of the fiber protein to a primary receptor (usually CAR or CD46). This event is followed by the engagement of the penton base protein ...Adenovirus (Ad) cell attachment is initiated by the attachment of the fiber protein to a primary receptor (usually CAR or CD46). This event is followed by the engagement of the penton base protein with a secondary receptor (integrin) via its loop region, which contains an Arg-Gly-Asp (RGD) motif, to trigger virus internalization. To understand the well-orchestrated adenovirus cell attachment process that involves the fiber and the penton base, we reconstructed the structure of an Ad5F35 capsid, comprising an adenovirus type 5 (Ad5) capsid pseudotyped with an Ad35 fiber, at a resolution of approximately 4.2 Å. The fiber-penton base interaction in the cryo-electron microscopic (cryo-EM) structure of Ad5F35 is similar to that in the cryo-EM structure of Ad5, indicating that the fiber-penton base interaction of adenovirus is conserved. Our structure also confirms that the C-terminal segment of the fiber tail domain constitutes the bottom trunk of the fiber shaft. Based on the conserved fiber-penton base interaction, we have proposed a model for the interaction of Ad5F35 with its primary and secondary receptors. This model could provide insight for designing adenovirus gene delivery vectors.
History
DepositionAug 10, 2012-
Header (metadata) releaseJul 3, 2013-
Map releaseOct 16, 2013-
UpdateOct 16, 2013-
Current statusOct 16, 2013Processing site: RCSB / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 13
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 13
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 13
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_5467.map.gz / Format: CCP4 / Size: 897.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation4.2 Angstrom Cryo-EM reconstruction of Ad5F35
Voxel sizeX=Y=Z: 1.15 Å
Density
Contour LevelBy AUTHOR: 13.0 / Movie #1: 13
Minimum - Maximum-66.919540409999996 - 89.600265500000006
Average (Standard dev.)1.78658485 (±7.64361334)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-392-3920
Dimensions784784392
Spacing784784392
CellA: 901.6 Å / B: 901.6 Å / C: 450.8 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.151.151.15
M x/y/z784784392
origin x/y/z0.0000.0000.000
length x/y/z901.600901.600450.800
α/β/γ90.00090.00090.000
start NX/NY/NZ-150-1500
NX/NY/NZ301301151
MAP C/R/S123
start NC/NR/NS-392-3920
NC/NR/NS784784392
D min/max/mean-66.92089.6001.787

-
Supplemental data

-
Segmentation: Ad5F35 monomer averaged from the 12 hexon monomers...

AnnotationAd5F35 monomer averaged from the 12 hexon monomers in an asymmetric unit of the icosahedron
Fileemd_5467_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Ad5F35--human adenovirus type 5 (Ad5) capsid pseudo-typed with an...

EntireName: Ad5F35--human adenovirus type 5 (Ad5) capsid pseudo-typed with an Ad35 fiber
Components
  • Sample: Ad5F35--human adenovirus type 5 (Ad5) capsid pseudo-typed with an Ad35 fiber
  • Virus: Human adenovirus 5

-
Supramolecule #1000: Ad5F35--human adenovirus type 5 (Ad5) capsid pseudo-typed with an...

SupramoleculeName: Ad5F35--human adenovirus type 5 (Ad5) capsid pseudo-typed with an Ad35 fiber
type: sample / ID: 1000 / Number unique components: 7

-
Supramolecule #1: Human adenovirus 5

SupramoleculeName: Human adenovirus 5 / type: virus / ID: 1 / NCBI-ID: 28285 / Sci species name: Human adenovirus 5 / Database: NCBI / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No
Host (natural)Organism: Homo sapiens (human) / synonym: VERTEBRATES
Virus shellShell ID: 1 / Diameter: 930 Å

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

VitrificationCryogen name: NITROGEN / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 75000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
DateOct 9, 2010
Image recordingCategory: CCD / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k) / Number real images: 4500 / Average electron dose: 20 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Final reconstructionAlgorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: IMIRS, recISAFs / Number images used: 2100
DetailsViruses in the grid with thin ice were imaged with an FEI 300-kV Titan Krios cryoelectron microscope equipped with a Gatan UltraScan4000 (model 895) 16-megapixel CCD.

-
Atomic model buiding 1

Initial modelPDB ID:

3iyn
PDB Unreleased entry

SoftwareName: Chimera
RefinementSpace: REAL

+
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