8FNE

phiPA3 PhuN Tetramer, p2

8FNE の概要

• エントリーDOI: 10.2210/pdb8fne/pdb
• 関連するPDBエントリー: 8FV5
• EMDBエントリー: 29310 29451 29550
• 分子名称: Maltose/maltodextrin-binding periplasmic protein, PhuN (1 entity in total)
• 機能のキーワード: phipa3 protein, shell protein, phun, phage nucleus, viral protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 881008.62

構造登録者

Nieweglowska, E.S.,Brilot, A.F.,Mendez-Moran, M.,Kokontis, C.,Baek, M.,Li, J.,Cheng, Y.,Baker, D.,Bondy-Denomy, J.,Agard, D.A. (登録日: 2022-12-27, 公開日: 2023-03-01, 最終更新日: 2024-06-19)

主引用文献

Nieweglowska, E.S.,Brilot, A.F.,Mendez-Moran, M.,Kokontis, C.,Baek, M.,Li, J.,Cheng, Y.,Baker, D.,Bondy-Denomy, J.,Agard, D.A.
The phi PA3 phage nucleus is enclosed by a self-assembling 2D crystalline lattice.
Nat Commun, 14:927-927, 2023

PubMed Abstract: To protect themselves from host attack, numerous jumbo bacteriophages establish a phage nucleus-a micron-scale, proteinaceous structure encompassing the replicating phage DNA. Bacteriophage and host proteins associated with replication and transcription are concentrated inside the phage nucleus while other phage and host proteins are excluded, including CRISPR-Cas and restriction endonuclease host defense systems. Here, we show that nucleus fragments isolated from ϕPA3 infected Pseudomonas aeruginosa form a 2-dimensional lattice, having p2 or p4 symmetry. We further demonstrate that recombinantly purified primary Phage Nuclear Enclosure (PhuN) protein spontaneously assembles into similar 2D sheets with p2 and p4 symmetry. We resolve the dominant p2 symmetric state to 3.9 Å by cryo-EM. Our structure reveals a two-domain core, organized into quasi-symmetric tetramers. Flexible loops and termini mediate adaptable inter-tetramer contacts that drive subunit assembly into a lattice and enable the adoption of different symmetric states. While the interfaces between subunits are mostly well packed, two are open, forming channels that likely have functional implications for the transport of proteins, mRNA, and small molecules.

PubMed: 36807264
DOI: 10.1038/s41467-023-36526-9

実験手法

ELECTRON MICROSCOPY (3.9 Å)