7N52

Structure of a bacterial gasdermin from Runella zeae

これはPDB形式変換不可エントリーです。

7N52 の概要

• エントリーDOI: 10.2210/pdb7n52/pdb
• 分子名称: Gasdermin (1 entity in total)
• 機能のキーワード: gasdermin, immunity, membrane, pore-forming protein, lipid binding protein, palmitoylation, immune system
• 由来する生物種: Runella zeae
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 122809.92

構造登録者

Johnson, A.G.,Kranzusch, P.J. (登録日: 2021-06-04, 公開日: 2021-06-23, 最終更新日: 2022-01-26)

主引用文献

Johnson, A.G.,Wein, T.,Mayer, M.L.,Duncan-Lowey, B.,Yirmiya, E.,Oppenheimer-Shaanan, Y.,Amitai, G.,Sorek, R.,Kranzusch, P.J.
Bacterial gasdermins reveal an ancient mechanism of cell death.
Science, 375:221-225, 2022

PubMed Abstract: Gasdermin proteins form large membrane pores in human cells that release immune cytokines and induce lytic cell death. Gasdermin pore formation is triggered by caspase-mediated cleavage during inflammasome signaling and is critical for defense against pathogens and cancer. We discovered gasdermin homologs encoded in bacteria that defended against phages and executed cell death. Structures of bacterial gasdermins revealed a conserved pore-forming domain that was stabilized in the inactive state with a buried lipid modification. Bacterial gasdermins were activated by dedicated caspase-like proteases that catalyzed site-specific cleavage and the removal of an inhibitory C-terminal peptide. Release of autoinhibition induced the assembly of large and heterogeneous pores that disrupted membrane integrity. Thus, pyroptosis is an ancient form of regulated cell death shared between bacteria and animals.

PubMed: 35025633
DOI: 10.1126/science.abj8432

実験手法

X-RAY DIFFRACTION (2.9 Å)