7UYX
Structure of bacteriophage PA1c gp2
7UYX の概要
エントリーDOI | 10.2210/pdb7uyx/pdb |
分子名称 | Bacteriophage PA1C gp2 (1 entity in total) |
機能のキーワード | jumbo phage nuclear shell, chimallin, viral protein |
由来する生物種 | Pseudomonas phage PA1C |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 88583.54 |
構造登録者 | Enustun, E.,Deep, A.,Gu, Y.,Nguyen, K.,Chaikeeratisak, V.,Armbruster, E.,Ghassemian, M.,Pogliano, J.,Corbett, K.D. (登録日: 2022-05-07, 公開日: 2023-05-10, 最終更新日: 2024-04-10) |
主引用文献 | Enustun, E.,Deep, A.,Gu, Y.,Nguyen, K.T.,Chaikeeratisak, V.,Armbruster, E.,Ghassemian, M.,Villa, E.,Pogliano, J.,Corbett, K.D. Identification of the bacteriophage nucleus protein interaction network. Nat.Struct.Mol.Biol., 30:1653-1662, 2023 Cited by PubMed Abstract: In the arms race between bacteria and bacteriophages (phages), some large-genome jumbo phages have evolved a protein shell that encloses their replicating genome to protect it against host immune factors. By segregating the genome from the host cytoplasm, however, the 'phage nucleus' introduces the need to specifically translocate messenger RNA and proteins through the nuclear shell and to dock capsids on the shell for genome packaging. Here, we use proximity labeling and localization mapping to systematically identify proteins associated with the major nuclear shell protein chimallin (ChmA) and other distinctive structures assembled by these phages. We identify six uncharacterized nuclear-shell-associated proteins, one of which directly interacts with self-assembled ChmA. The structure and protein-protein interaction network of this protein, which we term ChmB, suggest that it forms pores in the ChmA lattice that serve as docking sites for capsid genome packaging and may also participate in messenger RNA and/or protein translocation. PubMed: 37667030DOI: 10.1038/s41594-023-01094-5 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.63 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード