8IGG
C2 reconstruction of the concave tetramer in the cube-like assembly of 201Phi2-1 gp105
Summary for 8IGG
| Entry DOI | 10.2210/pdb8igg/pdb |
| EMDB information | 35432 |
| Descriptor | Chimallin (1 entity in total) |
| Functional Keywords | jumbo phage 201phi2-1, gp105, nucleus-like structure., structural protein |
| Biological source | Pseudomonas phage 201phi2-1 |
| Total number of polymer chains | 4 |
| Total formula weight | 282618.06 |
| Authors | |
| Primary citation | Liu, Z.,Xiang, Y. Structural studies of the nucleus-like assembly of jumbo bacteriophage 201 phi 2-1. Front Microbiol, 14:1170112-1170112, 2023 Cited by 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 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. PubMed: 37138628DOI: 10.3389/fmicb.2023.1170112 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.09 Å) |
Structure validation
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