7N35

Structure of Yersinia aleksiciae Cap15 cyclic dinucleotide receptor, crystal form 2

Summary for 7N35

• Entry DOI: 10.2210/pdb7n35/pdb
• Descriptor: Cap15 (1 entity in total)
• Functional Keywords: phage defense, cbass, beta barrel, immune system
• Biological source: Yersinia aleksiciae
• Total number of polymer chains: 2
• Total formula weight: 29993.28

Authors

Duncan-Lowey, B.,McNamara-Bordewick, N.K.,Kranzusch, P.J. (deposition date: 2021-05-31, release date: 2021-11-17, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)