[English] 日本語
Yorodumi
- EMDB-60197: Portal-tail of Vibrio cholerae typing phage mature VP1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-60197
TitlePortal-tail of Vibrio cholerae typing phage mature VP1
Map data
Sample
  • Virus: Vibrio cholerae phage (bacteria)
    • Protein or peptide: nozzle gp16
    • Protein or peptide: portal gp5
    • Protein or peptide: adaptor gp12
    • Protein or peptide: ring protein gp10
    • Protein or peptide: gp13
Keywordsphage / virus / vibrio cholera phage / VIRAL PROTEIN
Biological speciesVibrio cholerae (bacteria) / Vibrio cholerae phage (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsLiu HR / Pang H
Funding support China, 3 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)12034006 China
National Natural Science Foundation of China (NSFC)32071209 China
National Natural Science Foundation of China (NSFC)32200994 China
CitationJournal: Structure / Year: 2024
Title: Three-dimensional structures of Vibrio cholerae typing podophage VP1 in two states.
Authors: Hao Pang / Fenxia Fan / Jing Zheng / Hao Xiao / Zhixue Tan / Jingdong Song / Biao Kan / Hongrong Liu /
Abstract: Lytic podophages (VP1-VP5) play crucial roles in subtyping Vibrio cholerae O1 biotype El Tor. However, until now no structures of these phages have been available, which hindered our understanding of ...Lytic podophages (VP1-VP5) play crucial roles in subtyping Vibrio cholerae O1 biotype El Tor. However, until now no structures of these phages have been available, which hindered our understanding of the molecular mechanisms of infection and DNA release. Here, we determined the cryoelectron microscopy (cryo-EM) structures of mature and DNA-ejected VP1 structures at near-atomic and subnanometer resolutions, respectively. The VP1 head is composed of 415 copies of the major capsid protein gp7 and 11 turret-shaped spikes. The VP1 tail consists of an adapter, a nozzle, a slender ring, and a tail needle, and is flanked by three extended fibers I and six trimeric fibers II. Conformational changes of fiber II in DNA-ejected VP1 may cause the release of the tail needle and core proteins, forming an elongated tail channel. Our structures provide insights into the molecular mechanisms of infection and DNA release for podophages with a tail needle.
History
DepositionMay 16, 2024-
Header (metadata) releaseAug 14, 2024-
Map releaseAug 14, 2024-
UpdateDec 18, 2024-
Current statusDec 18, 2024Processing site: PDBj / Status: Released

-
Structure visualization

Supplemental images

emd_60197.png

Downloads & links

-
Map

FileDownload / File: emd_60197.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 400 pix.
= 440. Å		1.1 Å/pix.
x 400 pix.
= 440. Å		1.1 Å/pix.
x 400 pix.
= 440. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.7
Minimum - Maximum-7.103951 - 15.619445000000001
Average (Standard dev.)0.005217925 (±0.83986515)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-200-200-200
Dimensions400400400
Spacing400400400
CellA=B=C: 440.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_60197_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: #1

Fileemd_60197_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : Vibrio cholerae phage

EntireName: Vibrio cholerae phage (bacteria)
Components
  • Virus: Vibrio cholerae phage (bacteria)
    • Protein or peptide: nozzle gp16
    • Protein or peptide: portal gp5
    • Protein or peptide: adaptor gp12
    • Protein or peptide: ring protein gp10
    • Protein or peptide: gp13

-
Supramolecule #1: Vibrio cholerae phage

SupramoleculeName: Vibrio cholerae phage / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 666 / Sci species name: Vibrio cholerae phage / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No

-
Macromolecule #1: nozzle gp16

MacromoleculeName: nozzle gp16 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae (bacteria)
Molecular weightTheoretical: 59.015762 KDa
SequenceString: MEVTHKQFDL SGFLPDQAPD TLKSGAISRG FNVKPTILGW EKSGGFRETN TAPTNEKDFI FFWSPAIGDN RWFSGGDKTV QQVEGNVVS DVSRTGGYTA GSGRRWNAVN FNGVLLMNNE LDSPQYLAAS GKLEDFPNLP SNVRFRTVAV YKNFILGLGV N FGSGFLDD ...String:
MEVTHKQFDL SGFLPDQAPD TLKSGAISRG FNVKPTILGW EKSGGFRETN TAPTNEKDFI FFWSPAIGDN RWFSGGDKTV QQVEGNVVS DVSRTGGYTA GSGRRWNAVN FNGVLLMNNE LDSPQYLAAS GKLEDFPNLP SNVRFRTVAV YKNFILGLGV N FGSGFLDD EIYWSHQADP GTMPPNWDYA NAASDSGRTP LPSEGYCVTS EELGSMNIVY KSDSIWTMQL IGGQWIFRFE NK FPGQGIL NKKSVVSFEG KHFVVTQKDI IVHDGYQVRS VADKRVRNFF FTDMNSDYFE RVFVVKDPRV AEVYVFYPSK NSV DGLCDR ALVWNWRDDV WSLLNLRPLK HAAYGYEITG VSITWDNFVG GWESTGLWQA DEDVAKYAPV LHYSFRDVPK LLAP TPQAL FIDEEIEAVW EREDIVIGSI SRDGVPYQDY ERNKSVSSIS FDVDTTEPFD VYIGYKGSLE DSVEWEFAGT VNPME DKRL FCLLTAGLFS MRIISKAQTF ILRSYKITYE FAGEMWS

-
Macromolecule #2: portal gp5

MacromoleculeName: portal gp5 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae (bacteria)
Molecular weightTheoretical: 73.263602 KDa
SequenceString: MEILYTGASE SLHSTILKAL LERIDLGDTF ISDNYTRWQA TERYYMMYKI PNKKDKAAIE KWNKGDTDFK SLVMPYSYAQ LMTAHAYMV NVFLNRDPIF QTDSLNGDGT ERELALESML QYQVKAGEME PSLLVWFMDA LRYGVGVLGD YWEEHVFHQT V FEEEEEII ...String:
MEILYTGASE SLHSTILKAL LERIDLGDTF ISDNYTRWQA TERYYMMYKI PNKKDKAAIE KWNKGDTDFK SLVMPYSYAQ LMTAHAYMV NVFLNRDPIF QTDSLNGDGT ERELALESML QYQVKAGEME PSLLVWFMDA LRYGVGVLGD YWEEHVFHQT V FEEEEEII DGVPTGNMKK VKKTRVVKGY EGCKTFNVMV YDFIPDPRVA LCKYQEGEFF GRRLDLNVLD LKKGAKFGKY FN VEHAEAL VAASKEEMYR RDPSIGQQRS LKDSTMTPKG KQVGDISCVE IFVRLVPKDW GLGDSEFPEM WVFTVADKKY IVA AEPVNT LDDKFPFHIL ECEIDGYMNK SRGLLEISAP MNDILTWLFD SHMYNKRQIM NNQFIGDPSA LVVKDVESKE PGKF IRLRP TAYGRDVRSI ISQLPVTDVT AQNIQDVQVV ERNMQRIVGV NDDVAGQSSP SSRRSATEFR GTTSFASSRL ANLAY FFSV TGFRSLAKSL IVKTQQLYTV EMKVKVAGDN IKGAQSIIVK PEDISGQFDI MPVDGTLPVD RMAQAQFWMQ IMSMVA GNP VLGAEYRLGD IFSYTARLAG LKGIDKMKIR ILDDDQILAL ILAQQKGGAD VQPTGQPTTQ GVGNPTGVNE PAPSVTQ GT PGLSGLQALM

-
Macromolecule #3: adaptor gp12

MacromoleculeName: adaptor gp12 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae (bacteria)
Molecular weightTheoretical: 23.59285 KDa
SequenceString: MDKATLVKTI AYRMGNVKGQ DTAIDFELAL SIERLEGQEF VPWFLLSENN FFEGTAQENR IPVPRGFIRE YEEGSLYLRR VAGTGKCLI KKSQDQLLKY EGMTGEPSHY SLTNQYFRIY PVPQEDFKVE LLFYRKSSTL NVEDNPWYEY AAELLVAETI W AMLSARRD ...String:
MDKATLVKTI AYRMGNVKGQ DTAIDFELAL SIERLEGQEF VPWFLLSENN FFEGTAQENR IPVPRGFIRE YEEGSLYLRR VAGTGKCLI KKSQDQLLKY EGMTGEPSHY SLTNQYFRIY PVPQEDFKVE LLFYRKSSTL NVEDNPWYEY AAELLVAETI W AMLSARRD KMADYWKSVA ADQMRRLTIL DAERRLANQE IFMG

-
Macromolecule #4: ring protein gp10

MacromoleculeName: ring protein gp10 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae (bacteria)
Molecular weightTheoretical: 26.311119 KDa
SequenceString: MSSWDRFDTP WDSIIDESTW EHYTFKYDAS FEAFSSMEVD EDLTITVSVL FASTSDNTVT VGQVLGLTMD NRAGSYFGAG SSWTSEAAV NNEAGSGFQS SHALQLSYSV EDGVISSFGS EAFCSFYNTV SFESSSDVQA AVNSLYNLDV LFSSGSGDSE Q HYVVFGET ...String:
MSSWDRFDTP WDSIIDESTW EHYTFKYDAS FEAFSSMEVD EDLTITVSVL FASTSDNTVT VGQVLGLTMD NRAGSYFGAG SSWTSEAAV NNEAGSGFQS SHALQLSYSV EDGVISSFGS EAFCSFYNTV SFESSSDVQA AVNSLYNLDV LFSSGSGDSE Q HYVVFGET ASFESLAEHE TSSQYITHVE CMFNSVVEFE VKTYDWGRPV KPVGSDWSTD TPVVGVWVNE IYNGNKDWGE S

-
Macromolecule #5: gp13

MacromoleculeName: gp13 / type: protein_or_peptide / ID: 5 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Vibrio cholerae (bacteria)
Molecular weightTheoretical: 10.025203 KDa
SequenceString:
MALETWDANS TPATLNTAWP EATDPLNKGD DHIRLLKTVV VNFWNKVFDG SKLKTAVVPA AVNSATAGSG FGGFRYQVVN NSDGTKTLR LFTS

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 32.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.6 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 47456
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

+
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