Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition.
Journal, issue, pages	bioRxiv, Year 2026
Publish date	May 25, 2026
Authors	Laura Schmitt / Amel Chaïb / Denis Ptchelkine / Eaazhisai Kandiah / Claire Le Marrec / Christian Cambillau / Adeline Goulet
PubMed 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.
External links	bioRxiv / PubMed:42244550 / PubMed Central
Methods	EM (tomography) / EM (single particle)
Resolution	2.6 - 4.3 Å
Structure data	EMDB-57915: Siphohage OE33PA upon binding to its Gram+ host cell surface (view 1) Method: EM (tomography) EMDB-57916: Siphohage OE33PA upon binding to its Gram+ host cell surface (view 2) Method: EM (tomography) EMDB-57918: Siphohage OE33PA upon binding to its Gram+ host cell surface (view 3) Method: EM (tomography) EMDB-57919: Siphohage OE33PA upon binding to its Gram+ host cell surface (view 4) Method: EM (tomography) EMDB-57920: Siphohage OE33PA upon binding to its Gram+ host cell surface (view 5) Method: EM (tomography) EMDB-57921: Siphohage OE33PA upon binding to its Gram+ host cell surface (view 6) Method: EM (tomography) EMDB-57922: Siphohage OE33PA upon binding to its Gram+ host cell surface (view 7) Method: EM (tomography) 58149 30ys EMDB-58149, PDB-30ys: Capsid of the Oenococcus oeni phage OE33PA Method: EM (single particle) / Resolution: 2.8 Å 58150 30yt EMDB-58150, PDB-30yt: Capsid-connector assembly of the phage OE33PA Method: EM (single particle) / Resolution: 3.6 Å 58151 30yu EMDB-58151, PDB-30yu: Connector and Major Tail Protein of the phage OE33PA Method: EM (single particle) / Resolution: 3.0 Å 58152 30yv EMDB-58152, PDB-30yv: Portal-adaptor asssembly of the phage OE33PA Method: EM (single particle) / Resolution: 2.6 Å 58153 30yw EMDB-58153, PDB-30yw: Stopper and tail terminator assembly of the phage OE33PA Method: EM (single particle) / Resolution: 2.8 Å EMDB-58154: DNA in the capsid-tail connector of the phage OE33PA (classification focused on the adaptor-stopper region) Method: EM (single particle) / Resolution: 3.3 Å EMDB-58155: DNA in the capsid-tail connector of the phage OE33PA (classification focused on the capsid-portal junction) Method: EM (single particle) / Resolution: 3.0 Å EMDB-58156: Adhesion device of the phage OE33PA (unsymmetrized 3D reconstruction) Method: EM (single particle) / Resolution: 3.1 Å 58157 30yx EMDB-58157, PDB-30yx: adhesion device (C3 symmetrized reconstruction) of the phage OE33PA Method: EM (single particle) / Resolution: 2.7 Å 58158 30yy EMDB-58158, PDB-30yy: C6 symmetrized reconstruction of the adhesion device of the phage OE33PA Method: EM (single particle) / Resolution: 2.7 Å 58159 30yz EMDB-58159, PDB-30yz: RBP trimer bound to a monomer of the distal tail protein of the phage OE33PA Method: EM (single particle) / Resolution: 3.5 Å 58160 30za EMDB-58160, PDB-30za: Part of the tail tube of the phage OE33PA Method: EM (single particle) / Resolution: 2.9 Å EMDB-58161: Conformational variability of the phage OE33PA adhesion device (State 1) Method: EM (single particle) / Resolution: 4.3 Å EMDB-58162: Conformational variability of the phage OE33PA adhesion device (State 2) Method: EM (single particle) / Resolution: 3.7 Å
Chemicals	ChemComp-CA: Unknown entry
Source	oenococcus phage phioe33pa (virus) Oenococcus oeni (bacteria)
Keywords	VIRAL PROTEIN / major capsid protein / siphophage / STRUCTURAL PROTEIN / portal protein / connector assembly / connector / major tail protein / adaptor protein / stopper protein / tail terminator / head to tail connector / Distal tail protein / tail-associated lysin / tape measure protein / distail tail protein / adhesion device / receptor-binding protein / tail tube