[English] 日本語
Yorodumi
- EMDB-58157: adhesion device (C3 symmetrized reconstruction) of the phage OE33PA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-58157
Titleadhesion device (C3 symmetrized reconstruction) of the phage OE33PA
Map datasharpened map
Sample
  • Virus: Oenococcus phage phiOE33PA (virus)
    • Protein or peptide: Major tail protein
    • Protein or peptide: Distal tail protein
    • Protein or peptide: tail-associated dlysin
    • Protein or peptide: tape measure protein
  • Ligand: CALCIUM ION
KeywordsDistal tail protein / tail-associated lysin / tape measure protein / major tail protein / STRUCTURAL PROTEIN / VIRAL PROTEIN
Biological speciesOenococcus phage phiOE33PA (virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.7 Å
AuthorsGoulet A / Cambillau C
Funding support France, 3 items
OrganizationGrant numberCountry
Agence Nationale de la Recherche (ANR)ANR-21-CE11-0018-01 France
Agence Nationale de la Recherche (ANR)ANR-10-INSB-05-02 France
Agence Nationale de la Recherche (ANR)ANR-17-EURE-0003 France
CitationJournal: bioRxiv / Year: 2026
Title: Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition.
Authors: Laura Schmitt / Amel Chaïb / Denis Ptchelkine / Eaazhisai Kandiah / Claire Le Marrec / Christian Cambillau / Adeline Goulet
Abstract: Bacteriophages (phages) infecting Gram-positive bacteria must bind to host receptors across thick cell walls to initiate infection, yet the underlying structural mechanisms remain unclear. Here, we ...Bacteriophages (phages) infecting Gram-positive bacteria must bind to host receptors across thick cell walls to initiate infection, yet the underlying structural mechanisms remain unclear. Here, we report cryo-electron microscopy structures of the siphophage OE33PA, providing the first atomic resolution view of a phage infecting this bacterium important for the wine industry. While the overall virion architecture is conserved, the adhesion device displays distinctive features. Its receptor-binding proteins adopt multiple orientations, revealing an intrinsically dynamic assembly. cryo-electron tomography captures distinct conformations upon host attachment, providing rare structural insight into interactions with Gram-positive hosts. Additionally, functional assays show that a highly mobile carbohydrate-binding module in the distal tail protein mediates host-specific binding. Furthermore, the tape measure protein, central to phage assembly and infectivity, adopts a hexameric organization, updating the prevailing trimeric model in siphophages. Together, these findings reveal a dynamic adhesion device in a phage infecting Gram-positive bacteria and highlight the structural and functional diversity of phages.
History
DepositionMay 18, 2026-
Header (metadata) releaseJun 17, 2026-
Map releaseJun 17, 2026-
UpdateJun 17, 2026-
Current statusJun 17, 2026Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

emd_58157.png

Downloads & links

-
Map

FileDownload / File: emd_58157.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharpened map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 400 pix.
= 335.6 Å		0.84 Å/pix.
x 400 pix.
= 335.6 Å		0.84 Å/pix.
x 400 pix.
= 335.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.839 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-0.6230439 - 1.011849
Average (Standard dev.)0.0024164356 (±0.04192208)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 335.6 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Additional map: raw map

Fileemd_58157_additional_1.map
Annotationraw map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: #2

Fileemd_58157_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: #1

Fileemd_58157_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : Oenococcus phage phiOE33PA

EntireName: Oenococcus phage phiOE33PA (virus)
Components
  • Virus: Oenococcus phage phiOE33PA (virus)
    • Protein or peptide: Major tail protein
    • Protein or peptide: Distal tail protein
    • Protein or peptide: tail-associated dlysin
    • Protein or peptide: tape measure protein
  • Ligand: CALCIUM ION

-
Supramolecule #1: Oenococcus phage phiOE33PA

SupramoleculeName: Oenococcus phage phiOE33PA / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 / NCBI-ID: 2201414 / Sci species name: Oenococcus phage phiOE33PA / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No

-
Macromolecule #1: Major tail protein

MacromoleculeName: Major tail protein / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Oenococcus phage phiOE33PA (virus)
Molecular weightTheoretical: 20.83099 KDa
SequenceString: MATVGLKLVQ LALVGPDGKI LTDATTGLSA NGVYAVDSGV FSAKTANITG LEAASTKVYG NNRVVDLQHT KGDSSVALDF NALPHDILM KILGQVSDGK GGYTQGDKPK VAMLITTDAL AEDGQVYFGF RQGEIINPDF NNGTDTTTDT RNDDNLTYSP L DNPDWNNN ...String:
MATVGLKLVQ LALVGPDGKI LTDATTGLSA NGVYAVDSGV FSAKTANITG LEAASTKVYG NNRVVDLQHT KGDSSVALDF NALPHDILM KILGQVSDGK GGYTQGDKPK VAMLITTDAL AEDGQVYFGF RQGEIINPDF NNGTDTTTDT RNDDNLTYSP L DNPDWNNN PGKLWYSNET GFTQDIMLAD VFQGYVA

-
Macromolecule #2: Distal tail protein

MacromoleculeName: Distal tail protein / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Oenococcus phage phiOE33PA (virus)
Molecular weightTheoretical: 71.7455 KDa
SequenceString: MFKLTNARGE TVDLNTNSLR AYTPTGLGLT LKNTYSAYQS AFIKTHTQID DPASNPLQLY IKFGDVKSHS YQSFSDFSEF LAYPPYTLA YTTDAGTWYR KANLQSITKT EIGGSTIIAA DRLNEAFILE FYTAWYQLQS EEYVSYSNDP NLGLYGKIYN T SIKRNATD ...String:
MFKLTNARGE TVDLNTNSLR AYTPTGLGLT LKNTYSAYQS AFIKTHTQID DPASNPLQLY IKFGDVKSHS YQSFSDFSEF LAYPPYTLA YTTDAGTWYR KANLQSITKT EIGGSTIIAA DRLNEAFILE FYTAWYQLQS EEYVSYSNDP NLGLYGKIYN T SIKRNATD DSVSFPDQTL INSSGIDLAS IHDNGSATGT IQVSGSSEIQ NALVSVKDND GNIVGSQQLN TLPNPDQTVA AP SDTIIIH DNSDGSSTLS TKVTAGQSIQ LTQNTVGLIY SQANLGYNNL TADSEMLLGL QSASTAGWNS ANTISTILSG VYT DSVGKT HNAIQMASTS ASTSNVVVSK NIVPTLNSTY YWSVWYKVTG ALSTAASVHL EGRGIVSGSD AGTEAEALIS TTTA VGNWI QLTGSFTPTS SSTTYLRLRF QNLGTGTILF SEPMINSGSQ LNAYISDTVD ATQWSLKVTD GYLYLMEINA HEVDF TVLP QNTGYNFNFT FPHASGNYIF DNGSETFAFI LGSNLNYLFP YTYIESGRNL NQKAIPVSNS SEYFGLQNGS PCLITI TGP TTTNVSWEVL QNGITIASDA FDVTLTDNQQ LVVSSYPEDQ YARIYNPDGS YVNISQYQDI TKTNYILIPE GDSTIVF YI DKTAGVQLTY KEERLLV

-
Macromolecule #3: tail-associated dlysin

MacromoleculeName: tail-associated dlysin / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Oenococcus phage phiOE33PA (virus)
Molecular weightTheoretical: 39.169453 KDa
SequenceString: SLSLQATIFK ADLTIRGIYP VLSYSLSMDA VQNTSSTFVL YDSGVSQLGD YIAIKIANTN TLLYYGQLTA VDMDDSTSLD TLTANYIWN ALNGEIMVLG RSGQSYEIHI QKLIAQYIAS NSGNIFGHSV TTSTTTAYAI TTSDGVETSN FIDYLIRGFK L HNVVIRIK ...String:
SLSLQATIFK ADLTIRGIYP VLSYSLSMDA VQNTSSTFVL YDSGVSQLGD YIAIKIANTN TLLYYGQLTA VDMDDSTSLD TLTANYIWN ALNGEIMVLG RSGQSYEIHI QKLIAQYIAS NSGNIFGHSV TTSTTTAYAI TTSDGVETSN FIDYLIRGFK L HNVVIRIK DIKQGMSNGI PFYYPEFDIH QVTDSWNFKN NIYNFTNWTI SDSRLLRGYN NELWIVDKAS TNMESPSIIA KY WLQSDGT VVSSLNDNVS QPTQVHVYLY DKTATDNPSN DSIASTELSG NTYSHDIQFS MPIDNNFFPL SKLHLGLQSN IYY NGKLYK SVLSGYSLTS DSGLMTVEFG NLRFG

-
Macromolecule #4: tape measure protein

MacromoleculeName: tape measure protein / type: protein_or_peptide / ID: 4 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Oenococcus phage phiOE33PA (virus)
Molecular weightTheoretical: 6.024879 KDa
SequenceString:
NSKVETLLGQ NNQLINVLTN VVGSILGEVK AGNQKLTPGQ QATLTKNIIS MIGRSTN

-
Macromolecule #5: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 5 / Number of copies: 6 / Formula: CA
Molecular weightTheoretical: 40.078 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 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: 0.8 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: 2.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryospa / Number images used: 35755
Initial angle assignmentType: RANDOM ASSIGNMENT
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