[English] 日本語
Yorodumi
- EMDB-48460: Structure of the middle part of the bacteriophage T4 tail -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-48460
TitleStructure of the middle part of the bacteriophage T4 tail
Map data3-fold-symmetric reconstruction focused on the middle part of the phage tail
Sample
  • Virus: Escherichia phage T4 (virus)
    • Protein or peptide: gp18, tail sheath protein
    • Protein or peptide: gp19, tail tube protein
Keywordsbacteriophage T4 / contractile phage tail / sheath protein / tail tube protein / VIRUS / VIRAL PROTEIN
Function / homology
Function and homology information


virus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / structural molecule activity
Similarity search - Function
: / Tail sheath protein Gp18-like domain I / : / Tail sheath protein Gp18 domain III N-terminal region / Phage tail sheath protein, beta-sandwich domain / Phage tail sheath protein beta-sandwich domain / Bacteriophage T4, Gp19, tail tube / T4-like virus tail tube protein gp19 / : / Tail sheath protein, subtilisin-like domain ...: / Tail sheath protein Gp18-like domain I / : / Tail sheath protein Gp18 domain III N-terminal region / Phage tail sheath protein, beta-sandwich domain / Phage tail sheath protein beta-sandwich domain / Bacteriophage T4, Gp19, tail tube / T4-like virus tail tube protein gp19 / : / Tail sheath protein, subtilisin-like domain / Phage tail sheath protein subtilisin-like domain / Tail sheath protein, C-terminal domain / Phage tail sheath C-terminal domain
Similarity search - Domain/homology
Tail tube protein / Tail sheath protein
Similarity search - Component
Biological speciesEscherichia phage T4 (virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsFokine A / Zhu J / Klose T / Vago F / Arnaud C / Wang Z / Khare B / Rossmann MG / Chen Z / Sun L ...Fokine A / Zhu J / Klose T / Vago F / Arnaud C / Wang Z / Khare B / Rossmann MG / Chen Z / Sun L / Fang Q / Kuhn R / Rao VB
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI081726 United States
CitationJournal: To Be Published
Title: In situ Atomic Structure of Phage T4 Head-Tail Connector Complex Shows Molecular Gates Open for Genome Ejection and DNA Pushed into the Tail Tube
Authors: Fokine A / Zhu J / Klose T / Vago F / Arnaud C / Wang Z / Khare B / Rossmann MG / Chen Z / Sun L / Fang Q / Kuhn R / Rao VB
History
DepositionDec 26, 2024-
Header (metadata) releaseJan 28, 2026-
Map releaseJan 28, 2026-
UpdateJan 28, 2026-
Current statusJan 28, 2026Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_48460.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation3-fold-symmetric reconstruction focused on the middle part of the phage tail
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.62 Å/pix.
x 400 pix.
= 646.4 Å
1.62 Å/pix.
x 400 pix.
= 646.4 Å
1.62 Å/pix.
x 400 pix.
= 646.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.616 Å
Density
Contour LevelBy AUTHOR: 0.016
Minimum - Maximum-0.058421735 - 0.09635798
Average (Standard dev.)0.000017207425 (±0.004848805)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 646.4 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Mask #1

Fileemd_48460_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: half map B

Fileemd_48460_half_map_1.map
Annotationhalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: half map A

Fileemd_48460_half_map_2.map
Annotationhalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Escherichia phage T4

EntireName: Escherichia phage T4 (virus)
Components
  • Virus: Escherichia phage T4 (virus)
    • Protein or peptide: gp18, tail sheath protein
    • Protein or peptide: gp19, tail tube protein

-
Supramolecule #1: Escherichia phage T4

SupramoleculeName: Escherichia phage T4 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2681598 / Sci species name: Escherichia phage T4 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No
Host (natural)Organism: Escherichia coli (E. coli) / Strain: B

-
Macromolecule #1: gp18, tail sheath protein

MacromoleculeName: gp18, tail sheath protein / type: protein_or_peptide / ID: 1 / Number of copies: 84 / Enantiomer: LEVO
Source (natural)Organism: Escherichia phage T4 (virus)
Molecular weightTheoretical: 71.348625 KDa
SequenceString: MTLLSPGIEL KETTVQSTVV NNSTGTAALA GKFQWGPAFQ IKQVTNEVDL VNTFGQPTAE TADYFMSAMN FLQYGNDLRV VRAVDRDTA KNSSPIAGNI EYTISTPGSN YAVGDKITVK YVSDDIETEG KITEVDADGK IKKINIPTAK IIAKAKEVGE Y PTLGSNWT ...String:
MTLLSPGIEL KETTVQSTVV NNSTGTAALA GKFQWGPAFQ IKQVTNEVDL VNTFGQPTAE TADYFMSAMN FLQYGNDLRV VRAVDRDTA KNSSPIAGNI EYTISTPGSN YAVGDKITVK YVSDDIETEG KITEVDADGK IKKINIPTAK IIAKAKEVGE Y PTLGSNWT AEISSSSSGL AAVITLGKII TDSGILLAEI ENAEAAMTAV DFQANLKKYG IPGVVALYPG ELGDKIEIEI VS KADYAKG ASALLPIYPG GGTRASTAKA VFGYGPQTDS QYAIIVRRND AIVQSVVLST KRGGKDIYDS NIYIDDFFAK GGS EYIFAT AQNWPEGFSG ILTLSGGLSS NAEVTAGDLM EAWDFFADRE SVDVQLFIAG SCAGESLETA STVQKHVVSI GDVR QDCLV LCSPPRETVV GIPVTRAVDN LVNWRTAAGS YTDNNFNISS TYAAIDGNYK YQYDKYNDVN RWVPLAADIA GLCAR TDNV SQTWMSPAGY NRGQILNVIK LAIETRQAQR DRLYQEAINP VTGTGGDGYV LYGDKTATSV PSPFDRINVR RLFNML KTN IGRSSKYRLF ELNNAFTRSS FRTETAQYLQ GIKALGGIYE YRVVCDTTNN TPSVIDRNEF VATFYIQPAR SINYITL NF VATATGADFD ELTGLAG

UniProtKB: Tail sheath protein

-
Macromolecule #2: gp19, tail tube protein

MacromoleculeName: gp19, tail tube protein / type: protein_or_peptide / ID: 2 / Number of copies: 78 / Enantiomer: LEVO
Source (natural)Organism: Escherichia phage T4 (virus)
Molecular weightTheoretical: 18.479613 KDa
SequenceString:
MFVDDVTRAF ESGDFARPNL FQVEISYLGQ NFTFQCKATA LPAGIVEKIP VGFMNRKINV AGDRTFDDWT VTVMNDEAHD ARQKFVDWQ SIAAGQGNEI TGGKPAEYKK SAIVRQYARD AKTVTKEIEI KGLWPTNVGE LQLDWDSNNE IQTFEVTLAL D YWE

UniProtKB: Tail tube protein

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
GridModel: PELCO Ultrathin Carbon with Lacey Carbon / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: LACEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
Details: Ted Pella lacey carbon 400 mesh grids (catalog No: 01824) were used..

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 38.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.6 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 113800
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

+
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