7n35 | pdb_00007n35

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

spinqualitylabelsall models 7n35, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7n35 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 beta-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. Effector-mediated membrane disruption controls cell death in CBASS antiphage defense.,Duncan-Lowey B, McNamara-Bordewick NK, Tal N, Sorek R, Kranzusch PJ Mol Cell. 2021 Nov 9. pii: S1097-2765(21)00912-6. doi:, 10.1016/j.molcel.2021.10.020. PMID:34784509 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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