8IGG

C2 reconstruction of the concave tetramer in the cube-like assembly of 201Phi2-1 gp105

8IGG の概要

• エントリーDOI: 10.2210/pdb8igg/pdb
• EMDBエントリー: 35432
• 分子名称: Chimallin (1 entity in total)
• 機能のキーワード: jumbo phage 201phi2-1, gp105, nucleus-like structure., structural protein
• 由来する生物種: Pseudomonas phage 201phi2-1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 282618.06

構造登録者

Liu, Z.,Xiang, Y. (登録日: 2023-02-20, 公開日: 2023-05-03, 最終更新日: 2024-07-03)

主引用文献

Liu, Z.,Xiang, Y.
Structural studies of the nucleus-like assembly of jumbo bacteriophage 201 phi 2-1.
Front Microbiol, 14:1170112-1170112, 2023

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: 37138628
DOI: 10.3389/fmicb.2023.1170112

実験手法

ELECTRON MICROSCOPY (4.09 Å)