+
Open data
-
Basic information
| Entry | ![]() | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Part of the tail tube of the phage OE33PA | ||||||||||||
Map data | sharpened map | ||||||||||||
Sample |
| ||||||||||||
Keywords | Major tail protein / tail tube / siphophage / STRUCTURAL PROTEIN / VIRAL PROTEIN | ||||||||||||
| Biological species | Oenococcus phage phiOE33PA (virus) | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | ||||||||||||
Authors | Goulet A / Cambillau C | ||||||||||||
| Funding support | France, 3 items
| ||||||||||||
Citation | Journal: bioRxiv / Year: 2026Title: 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 |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_58160.map.gz | 230.2 MB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-58160-v30.xml emd-58160.xml | 18 KB 18 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_58160_fsc.xml | 13.2 KB | Display | FSC data file |
| Images | emd_58160.png | 133.6 KB | ||
| Filedesc metadata | emd-58160.cif.gz | 5.3 KB | ||
| Others | emd_58160_additional_1.map.gz emd_58160_half_map_1.map.gz emd_58160_half_map_2.map.gz | 203.9 MB 226.3 MB 226.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-58160 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-58160 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 30zaMC ![]() 30ysC ![]() 30ytC ![]() 30yuC ![]() 30yvC ![]() 30ywC ![]() 30yxC ![]() 30yyC ![]() 30yzC M: atomic model generated by this map C: citing same article ( |
|---|
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|
-
Map
| File | Download / File: emd_58160.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Annotation | sharpened map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.839 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-Additional map: raw map
| File | emd_58160_additional_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Annotation | raw map | ||||||||||||
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: #2
| File | emd_58160_half_map_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: #1
| File | emd_58160_half_map_2.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-
Sample components
-Entire : Oenococcus phage phiOE33PA
| Entire | Name: Oenococcus phage phiOE33PA (virus) |
|---|---|
| Components |
|
-Supramolecule #1: Oenococcus phage phiOE33PA
| Supramolecule | Name: Oenococcus phage phiOE33PA / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1 / 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
| Macromolecule | Name: Major tail protein / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
|---|---|
| Source (natural) | Organism: Oenococcus phage phiOE33PA (virus) |
| Molecular weight | Theoretical: 21.346514 KDa |
| Sequence | String: 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 VFQGYVAAAQ SAS |
-Macromolecule #2: CALCIUM ION
| Macromolecule | Name: CALCIUM ION / type: ligand / ID: 2 / Number of copies: 12 / Formula: CA |
|---|---|
| Molecular weight | Theoretical: 40.078 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
|---|---|
Processing | single particle reconstruction |
| Aggregation state | particle |
-
Sample preparation
| Buffer | pH: 7.5 |
|---|---|
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination 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 |
Movie
Controller
About Yorodumi




Oenococcus phage phiOE33PA (virus)
Keywords
Authors
France, 3 items
Citation




























Z (Sec.)
Y (Row.)
X (Col.)












































Processing
FIELD EMISSION GUN

