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Activation of CBASS Cap5 endonuclease immune effector by cyclic nucleotides

Nat Struct Mol Biol. 2024-02; 
Olga Rechkoblit, Daniela Sciaky, Dale F Kreitler, Angeliki Buku, Jithesh Kottur, Aneel K Aggarwal
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Molecular Biology Reagents … coli (Genscript) was inserted between the NdeI and HindIII cloning sites of the pET28b(+) vector. The plasmid was transformed into E. coli BL21 (DE3) competent cells. … Get A Quote

摘要

The bacterial cyclic oligonucleotide-based antiphage signaling system (CBASS) is similar to the cGAS-STING system in humans, containing an enzyme that synthesizes a cyclic nucleotide on viral infection and an effector that senses the second messenger for the antiviral response. Cap5, containing a SAVED domain coupled to an HNH DNA endonuclease domain, is the most abundant CBASS effector, yet the mechanism by which it becomes activated for cell killing remains unknown. We present here high-resolution structures of full-length Cap5 from Pseudomonas syringae (Ps) with second messengers. The key to PsCap5 activation is a dimer-to-tetramer transition, whereby the binding of second messenger to dimer triggers an open... More

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