8DGF

Avs4 bound to phage PhiV-1 portal

8DGF の概要

• エントリーDOI: 10.2210/pdb8dgf/pdb
• EMDBエントリー: 27422
• 分子名称: ATP-binding protein Avs4, Portal protein, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: phage defense, pattern-recognition receptor, nlr, stand, atpase, antiviral protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 982913.57

構造登録者

Wilkinson, M.E.,Gao, L.,Strecker, J.,Makarova, K.S.,Macrae, R.K.,Koonin, E.V.,Zhang, F. (登録日: 2022-06-23, 公開日: 2022-08-03, 最終更新日: 2025-05-21)

主引用文献

Gao, L.A.,Wilkinson, M.E.,Strecker, J.,Makarova, K.S.,Macrae, R.K.,Koonin, E.V.,Zhang, F.
Prokaryotic innate immunity through pattern recognition of conserved viral proteins.
Science, 377:eabm4096-eabm4096, 2022

PubMed Abstract: Many organisms have evolved specialized immune pattern-recognition receptors, including nucleotide-binding oligomerization domain-like receptors (NLRs) of the STAND superfamily that are ubiquitous in plants, animals, and fungi. Although the roles of NLRs in eukaryotic immunity are well established, it is unknown whether prokaryotes use similar defense mechanisms. Here, we show that antiviral STAND (Avs) homologs in bacteria and archaea detect hallmark viral proteins, triggering Avs tetramerization and the activation of diverse N-terminal effector domains, including DNA endonucleases, to abrogate infection. Cryo-electron microscopy reveals that Avs sensor domains recognize conserved folds, active-site residues, and enzyme ligands, allowing a single Avs receptor to detect a wide variety of viruses. These findings extend the paradigm of pattern recognition of pathogen-specific proteins across all three domains of life.

PubMed: 35951700
DOI: 10.1126/science.abm4096

実験手法

ELECTRON MICROSCOPY (2.9 Å)