[English] 日本語
Yorodumi
- EMDB-61909: core proteins of mature T7 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-61909
Titlecore proteins of mature T7
Map datacore proteins of T7
Sample
  • Virus: Escherichia phage T7 (virus)
    • Protein or peptide: Protein 6.7
    • Protein or peptide: Internal virion protein gp14
    • Protein or peptide: Internal virion protein gp15
    • Protein or peptide: Peptidoglycan transglycosylase gp16
KeywordsComplex / VIRAL PROTEIN
Function / homology
Function and homology information


symbiont genome ejection through host cell envelope / : / symbiont entry into host cell via disruption of host cell wall peptidoglycan / peptidoglycan lytic transglycosylase activity / symbiont genome ejection through host cell envelope, short tail mechanism / symbiont entry into host cell via disruption of host cell envelope / peptidoglycan metabolic process / symbiont entry into host / T=7 icosahedral viral capsid / virion component ...symbiont genome ejection through host cell envelope / : / symbiont entry into host cell via disruption of host cell wall peptidoglycan / peptidoglycan lytic transglycosylase activity / symbiont genome ejection through host cell envelope, short tail mechanism / symbiont entry into host cell via disruption of host cell envelope / peptidoglycan metabolic process / symbiont entry into host / T=7 icosahedral viral capsid / virion component / killing of cells of another organism / hydrolase activity / defense response to bacterium / host cell plasma membrane / membrane
Similarity search - Function
Bacteriophage T7-like, protein 6.7 / Bacteriophage T7-like, protein 6.7 / Internal virion protein Gp16 / Internal virion protein Gp14 / T7 virus internal virion protein gp14 family / Prokaryotic transglycosylase, active site / Prokaryotic transglycosylases signature. / Transglycosylase SLT domain 1 / Transglycosylase SLT domain / Lysozyme-like domain superfamily
Similarity search - Domain/homology
Internal virion protein gp14 / Peptidoglycan transglycosylase gp16 / Protein 6.7
Similarity search - Component
Biological speciesEscherichia phage T7 (virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsLiu HR / Chen WY
Funding support China, 6 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)12034006 China
National Natural Science Foundation of China (NSFC)32430020 China
National Natural Science Foundation of China (NSFC)32071209 China
National Natural Science Foundation of China (NSFC)32371263 China
National Natural Science Foundation of China (NSFC)32200994 China
National Natural Science Foundation of China (NSFC)32401014 China
CitationJournal: J Virol / Year: 2025
Title: Conformational changes in and translocation of small proteins: insights into the ejection mechanism of podophages.
Authors: Jing Zheng / Hao Xiao / Hao Pang / Li Wang / Jingdong Song / Wenyuan Chen / Lingpeng Cheng / Hongrong Liu /
Abstract: Podophage tails are too short to span the cell envelope during infection. Consequently, podophages initially eject the core proteins within the head for the formation of an elongated trans-envelope ...Podophage tails are too short to span the cell envelope during infection. Consequently, podophages initially eject the core proteins within the head for the formation of an elongated trans-envelope channel for DNA ejection. Although the core proteins of bacteriophage T7 have been resolved at near-atomic resolution, the mechanisms of core proteins and DNA ejection remain to be fully elucidated. In this study, we provided improved structures of core proteins in mature T7 and the portal-tail complex in lipopolysaccharide-induced DNA-ejected T7 to resolutions of approximately 3 Å. Using these structures, we identified three small proteins, namely gp14, gp6.7, and gp7.3, and illustrated the conformational changes in and translocation of these proteins from the mature to DNA-ejected states. Our structures indicate that gp6.7, which participates in the assembly of the core and trans-envelope channel, is a core protein, and that gp7.3 serves as a structural scaffold to assist the assembly of the nozzle into the adaptor.
IMPORTANCE: Podophage T7 core proteins form an elongated trans-envelope channel for genomic DNA delivery into the host cell. The structures of the core proteins within the mature T7 and assembled in ...IMPORTANCE: Podophage T7 core proteins form an elongated trans-envelope channel for genomic DNA delivery into the host cell. The structures of the core proteins within the mature T7 and assembled in the periplasmic tunnel form in the DNA-ejected T7 have been resolved previously. Here, we resolved the structures of two new structural proteins (gp6.7 and gp7.3) within mature T7 and receptor-induced DNA-ejected T7. The gp6.7 protein participates in the assembly of the core complex within mature T7 and the trans-envelope channel during T7 infection; therefore, gp6.7 is a core protein. Before T7 infection, gp7.3 plays a role in promoting the assembly of the nozzle into the adaptor.
History
DepositionOct 13, 2024-
Header (metadata) releaseDec 11, 2024-
Map releaseDec 11, 2024-
UpdateJun 25, 2025-
Current statusJun 25, 2025Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

emd_61909.png

Downloads & links

-
Map

FileDownload / File: emd_61909.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationcore proteins of T7
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 320 pix.
= 339.2 Å		1.06 Å/pix.
x 320 pix.
= 339.2 Å		1.06 Å/pix.
x 320 pix.
= 339.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 2.0
Minimum - Maximum-11.324947999999999 - 19.307162999999999
Average (Standard dev.)0.004073098 (±0.90823567)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-160-160-160
Dimensions320320320
Spacing320320320
CellA=B=C: 339.19998 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_61909_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: #1

Fileemd_61909_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : Escherichia phage T7

EntireName: Escherichia phage T7 (virus)
Components
  • Virus: Escherichia phage T7 (virus)
    • Protein or peptide: Protein 6.7
    • Protein or peptide: Internal virion protein gp14
    • Protein or peptide: Internal virion protein gp15
    • Protein or peptide: Peptidoglycan transglycosylase gp16

-
Supramolecule #1: Escherichia phage T7

SupramoleculeName: Escherichia phage T7 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10760 / Sci species name: Escherichia phage T7 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No

-
Macromolecule #1: Protein 6.7

MacromoleculeName: Protein 6.7 / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Escherichia phage T7 (virus)
Molecular weightTheoretical: 9.354512 KDa
SequenceString:
MCFSPKIKTP KMDTNQIRAV EPAPLTQEVS SVEFGGSSDE TDTEGTEVSG RKGLKVERDD SVAKSKASGN GSARMKSSIR KSAFGGKK

UniProtKB: Protein 6.7

-
Macromolecule #2: Internal virion protein gp14

MacromoleculeName: Internal virion protein gp14 / type: protein_or_peptide / ID: 2 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Escherichia phage T7 (virus)
Molecular weightTheoretical: 20.990842 KDa
SequenceString: MCWAAAIPIA ISGAQAISGQ NAQAKMIAAQ TAAGRRQAME IMRQTNIQNA DLSLQARSKL EEASAELTSQ NMQKVQAIGS IRAAIGESM LEGSSMDRIK RVTEGQFIRE ANMVTENYRR DYQAIFAQQL GGTQSAASQI DEIYKSEQKQ KSKLQMVLDP L AIMGSSAA ...String:
MCWAAAIPIA ISGAQAISGQ NAQAKMIAAQ TAAGRRQAME IMRQTNIQNA DLSLQARSKL EEASAELTSQ NMQKVQAIGS IRAAIGESM LEGSSMDRIK RVTEGQFIRE ANMVTENYRR DYQAIFAQQL GGTQSAASQI DEIYKSEQKQ KSKLQMVLDP L AIMGSSAA SAYASGAFDS KSTTKAPIVA AKGTKTGR

UniProtKB: Internal virion protein gp14

-
Macromolecule #3: Internal virion protein gp15

MacromoleculeName: Internal virion protein gp15 / type: protein_or_peptide / ID: 3 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Escherichia phage T7 (virus)
Molecular weightTheoretical: 84.454008 KDa
SequenceString: MSKIESALQA AQPGLSRLRG GAGGMGYRAA TTQAEQPRSS LLDTIGRFAK AGADMYTAKE QRARDLADER SNEIIRKLTP EQRREALNN GTLLYQDDPY AMEALRVKTG RNAAYLVDDD VMQKIKEGVF RTREEMEEYR HSRLQEGAKV YAEQFGIDPE D VDYQRGFN ...String:
MSKIESALQA AQPGLSRLRG GAGGMGYRAA TTQAEQPRSS LLDTIGRFAK AGADMYTAKE QRARDLADER SNEIIRKLTP EQRREALNN GTLLYQDDPY AMEALRVKTG RNAAYLVDDD VMQKIKEGVF RTREEMEEYR HSRLQEGAKV YAEQFGIDPE D VDYQRGFN GDITERNISL YGAHDNFLSQ QAQKGAIMNS RVELNGVLQD PDMLRRPDSA DFFEKYIDNG LVTGAIPSDA QA TQLISQA FSDASSRAGG ADFLMRVGDK KVTLNGATTT YRELIGEEQW NALMVTAQRS QFETDAKLNE QYRLKINSAL NQE DPRTAW EMLQGIKAEL DKVQPDEQMT PQREWLISAQ EQVQNQMNAW TKAQAKALDD SMKSMNKLDV IDKQFQKRIN GEWV STDFK DMPVNENTGE FKHSDMVNYA NKKLAEIDSM DIPDGAKDAM KLKYLQADSK DGAFRTAIGT MVTDAGQEWS AAVIN GKLP ERTPAMDALR RIRNADPQLI AALYPDQAEL FLTMDMMDKQ GIDPQVILDA DRLTVKRSKE QRFEDDKAFE SALNAS KAP EIARMPASLR ESARKIYDSV KYRSGNESMA MEQMTKFLKE STYTFTGDDV DGDTVGVIPK NMMQVNSDPK SWEQGRD IL EEARKGIIAS NPWITNKQLT MYSQGDSIYL MDTTGQVRVR YDKELLSKVW SENQKKLEEK AREKALADVN KRAPIVAA T KAREAAAKRV REKRKQTPKF IYGRKE

-
Macromolecule #4: Peptidoglycan transglycosylase gp16

MacromoleculeName: Peptidoglycan transglycosylase gp16 / type: protein_or_peptide / ID: 4 / Number of copies: 4 / Enantiomer: LEVO
EC number: Lyases; Carbon-oxygen lyases; Acting on polysaccharides
Source (natural)Organism: Escherichia phage T7 (virus)
Molecular weightTheoretical: 144.028219 KDa
SequenceString: MDKYDKNVPS DYDGLFQKAA DANGVSYDLL RKVAWTESRF VPTAKSKTGP LGMMQFTKAT AKALGLRVTD GPDDDRLNPE LAINAAAKQ LAGLVGKFDG DELKAALAYN QGEGRLGNPQ LEAYSKGDFA SISEEGRNYM RNLLDVAKSP MAGQLETFGG I TPKGKGIP ...String:
MDKYDKNVPS DYDGLFQKAA DANGVSYDLL RKVAWTESRF VPTAKSKTGP LGMMQFTKAT AKALGLRVTD GPDDDRLNPE LAINAAAKQ LAGLVGKFDG DELKAALAYN QGEGRLGNPQ LEAYSKGDFA SISEEGRNYM RNLLDVAKSP MAGQLETFGG I TPKGKGIP AEVGLAGIGH KQKVTQELPE STSFDVKGIE QEATAKPFAK DFWETHGETL DEYNSRSTFF GFKNAAEAEL SN SVAGMAF RAGRLDNGFD VFKDTITPTR WNSHIWTPEE LEKIRTEVKN PAYINVVTGG SPENLDDLIK LANENFENDS RAA EAGLGA KLSAGIIGAG VDPLSYVPMV GVTGKGFKLI NKALVVGAES AALNVASEGL RTSVAGGDAD YAGAALGGFV FGAG MSAIS DAVAAGLKRS KPEAEFDNEF IGPMMRLEAR ETARNANSAD LSRMNTENMK FEGEHNGVPY EDLPTERGAV VLHDG SVLS ASNPINPKTL KEFSEVDPEK AARGIKLAGF TEIGLKTLGS DDADIRRVAI DLVRSPTGMQ SGASGKFGAT ASDIHE RLH GTDQRTYNDL YKAMSDAMKD PEFSTGGAKM SREETRYTIY RRAALAIERP ELQKALTPSE RIVMDIIKRH FDTKREL ME NPAIFGNTKA VSIFPESRHK GTYVPHVYDR HAKALMIQRY GAEGLQEGIA RSWMNSYVSR PEVKARVDEM LKELHGVK E VTPEMVEKYA MDKAYGISHS DQFTNSSIIE ENIEGLVGIE NNSFLEARNL FDSDLSITMP DGQQFSVNDL RDFDMFRIM PAYDRRVNGD IAIMGSTGKT TKELKDEILA LKAKAEGDGK KTGEVHALMD TVKILTGRAR RNQDTVWETS LRAINDLGFF AKNAYMGAQ NITEIAGMIV TGNVRALGHG IPILRDTLYK SKPVSAKELK ELHASLFGKE VDQLIRPKRA DIVQRLREAT D TGPAVANI VGTLKYSTQE LAARSPWTKL LNGTTNYLLD AARQGMLGDV ISATLTGKTT RWEKEGFLRG ASVTPEQMAG IK SLIKEHM VRGEDGKFTV KDKQAFSMDP RAMDLWRLAD KVADEAMLRP HKVSLQDSHA FGALGKMVMQ FKSFTIKSLN SKF LRTFYD GYKNNRAIDA ALSIITSMGL AGGFYAMAAH VKAYALPKEK RKEYLERALD PTMIAHAALS RSSQLGAPLA MVDL VGGVL GFESSKMARS TILPKDTVKE RDPNKPYTSR EVMGAMGSNL LEQMPSAGFV ANVGATLMNA AGVVNSPNKA TEQDF MTGL MNSTKELVPN DPLTQQLVLK IYEANGVNLR ERRK

UniProtKB: Peptidoglycan transglycosylase gp16

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 35.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 45731
Initial angle assignmentType: COMMON LINE
Final angle assignmentType: PROJECTION MATCHING

+
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