7N34

Structure of Yersinia aleksiciae Cap15 cyclic dinucleotide receptor, crystal form 1

7N34 の概要

• エントリーDOI: 10.2210/pdb7n34/pdb
• 分子名称: Cap15 (2 entities in total)
• 機能のキーワード: phage defense, cbass, beta barrel, immune system
• 由来する生物種: Yersinia aleksiciae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15043.53

構造登録者

Duncan-Lowey, B.,McNamara-Bordewick, N.K.,Kranzusch, P.J. (登録日: 2021-05-31, 公開日: 2021-11-17, 最終更新日: 2024-10-30)

主引用文献

Duncan-Lowey, B.,McNamara-Bordewick, N.K.,Tal, N.,Sorek, R.,Kranzusch, P.J.
Effector-mediated membrane disruption controls cell death in CBASS antiphage defense.
Mol.Cell, 81:5039-, 2021

PubMed Abstract: Cyclic oligonucleotide-based antiphage signaling systems (CBASS) are antiviral defense operons that protect bacteria from phage replication. Here, we discover a widespread class of CBASS transmembrane (TM) effector proteins that respond to antiviral nucleotide signals and limit phage propagation through direct membrane disruption. Crystal structures of the Yersinia TM effector Cap15 reveal a compact 8-stranded β-barrel scaffold that forms a cyclic dinucleotide receptor domain that oligomerizes upon activation. We demonstrate that activated Cap15 relocalizes throughout the cell and specifically induces rupture of the inner membrane. Screening for active effectors, we identify the function of distinct families of CBASS TM effectors and demonstrate that cell death via disruption of inner-membrane integrity is a common mechanism of defense. Our results reveal the function of the most prominent class of effector protein in CBASS immunity and define disruption of the inner membrane as a widespread strategy of abortive infection in bacterial phage defense.

PubMed: 34784509
DOI: 10.1016/j.molcel.2021.10.020

実験手法

X-RAY DIFFRACTION (1.9 Å)