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| Title | Structural studies of the nucleus-like assembly of jumbo bacteriophage 201φ2-1. |
|---|---|
| Journal, issue, pages | Front Microbiol, Vol. 14, Page 1170112, Year 2023 |
| Publish date | Apr 17, 2023 |
 Authors | Zhe Liu / Ye Xiang /  |
| PubMed Abstract | The jumbo phages encode proteins that assemble to form a nucleus-like compartment in infected cells. Here we report the cryo-EM structure and biochemistry characterization of gp105, a protein that is ...The jumbo phages encode proteins that assemble to form a nucleus-like compartment in infected cells. Here we report the cryo-EM structure and biochemistry characterization of gp105, a protein that is encoded by the jumbo phage 201φ2-1 and is involved in the formation of the nucleus-like compartment in phage 201φ2-1 infected . We found that, although most gp105 molecules are in the monomeric state in solution, a small portion of gp105 assemble to form large sheet-like assemblies and small cube-like particles. Reconstruction of the cube-like particles showed that the particle consists of six flat head-to-tail tetramers arranged into an octahedral cube. The four molecules at the contact interface of two head-to-tail tetramers are 2-fold symmetry-related and constitute a concave tetramer. Further reconstructions without applying symmetry showed that molecules in the particles around the distal ends of a 3-fold axis are highly dynamic and have the tendency to open up the assembly. Local classifications and refinements of the concave tetramers in the cube-like particle resulted in a map of the concave tetramer at a resolution of 4.09 Å. Structural analysis of the concave tetramer indicates that the N and C terminal fragments of gp105 are important for mediating the intermolecular interactions, which was further confirmed by mutagenesis studies. Biochemistry assays showed that, in solution, the cube-like particles of gp105 are liable to either disassemble to form the monomers or recruit more molecules to form the high molecular weight lattice-like assembly. We also found that monomeric gp105s can self-assemble to form large sheet-like assemblies , and the assembly of gp105 is a reversible dynamic process and temperature-dependent. Taken together, our results revealed the dynamic assembly of gp105, which helps to understand the development and function of the nucleus-like compartment assembled by phage-encoded proteins. |
 External links | Front Microbiol / PubMed:37138628 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.09 - 6.41 Å |
| Structure data |  EMDB-35430: 201Phi2-1 gp105 cube-like assembly (C1, 24mer)  EMDB-35431: 201Phi2-1 gp105 cube-like assembly (O, 24mer) EMDB-35432, PDB-8igg: |
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 Keywords |  STRUCTURAL PROTEIN / jumbo phage 201phi2-1 / gp105 / nucleus-like structure. |
pseudomonas phage 201phi2-1 (virus)