7UYX

Structure of bacteriophage PA1c gp2

Summary for 7UYX

• Entry DOI: 10.2210/pdb7uyx/pdb
• Descriptor: Bacteriophage PA1C gp2 (1 entity in total)
• Functional Keywords: jumbo phage nuclear shell, chimallin, viral protein
• Biological source: Pseudomonas phage PA1C
• Total number of polymer chains: 4
• Total formula weight: 88583.54

Authors

Enustun, E.,Deep, A.,Gu, Y.,Nguyen, K.,Chaikeeratisak, V.,Armbruster, E.,Ghassemian, M.,Pogliano, J.,Corbett, K.D. (deposition date: 2022-05-07, release date: 2023-05-10, Last modification date: 2024-04-10)

Primary citation

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

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: 37667030
DOI: 10.1038/s41594-023-01094-5

Experimental method

X-RAY DIFFRACTION (2.63 Å)