Structural highlights
Function
CTEC_CHRVO ADP-ribosyltransferase that specifically modifies host ubiquitin on 'Thr-66' residue, which causes the shutdown of polyubiquitin synthesis and disrupts the recognition and reversal of polyubiquitin in host cells during infection (PubMed:32330457). Threonine ADP-ribosylation of ubiquitin prevents the transfer of ubiquitin from ubiquitin-activating enzyme E1 to ubiquitin-conjugating enzyme E2, which inhibits subsequent ubiquitin activation and leads to the shutdown of polyubiquitin synthesis in host cells (PubMed:32330457). The modification also causes dysfunction of polyubiquitin chains in cells, thereby blocking host ubiquitin signaling (PubMed:32330457). ADP-ribosylation by CteC is likely irreversible (PubMed:32330457). Plays a crucial role in bacterial colonization in mice during infection (PubMed:32330457).[1]
See Also
References
- ↑ Yan F, Huang C, Wang X, Tan J, Cheng S, Wan M, Wang Z, Wang S, Luo S, Li A, Guo X, Feng M, Liu X, Zhu Y, Zhou Y. Threonine ADP-Ribosylation of Ubiquitin by a Bacterial Effector Family Blocks Host Ubiquitination. Mol Cell. 2020 May 21;78(4):641-652.e9. doi: 10.1016/j.molcel.2020.03.016. Epub, 2020 Apr 23. PMID:32330457 doi:http://dx.doi.org/10.1016/j.molcel.2020.03.016
