Structural highlights
Function
THSB2_BACCS TIR-like domain-containing component of the Thoeris antiviral defense system, composed of ThsA and ThsB and ThsB' (Probable). In the presence of NAD(+) produces a signaling molecule that activates cognate ThsA (AC J8G6Z1) to hydrolyze NAD(+) (PubMed:36174646). The signaling molecule is a cyclic ADP-D-ribose isomer and may be 3' cyclic ADP-D-ribose (3'cADPR); it is not 2'cADPR (Probable).[1] [2]
References
- ↑ Leavitt A, Yirmiya E, Amitai G, Lu A, Garb J, Herbst E, Morehouse BR, Hobbs SJ, Antine SP, Sun ZJ, Kranzusch PJ, Sorek R. Viruses inhibit TIR gcADPR signalling to overcome bacterial defence. Nature. 2022 Nov;611(7935):326-331. PMID:36174646 doi:10.1038/s41586-022-05375-9
- ↑ Leavitt A, Yirmiya E, Amitai G, Lu A, Garb J, Herbst E, Morehouse BR, Hobbs SJ, Antine SP, Sun ZJ, Kranzusch PJ, Sorek R. Viruses inhibit TIR gcADPR signalling to overcome bacterial defence. Nature. 2022 Nov;611(7935):326-331. PMID:36174646 doi:10.1038/s41586-022-05375-9
