Crystal structure of Type VI immunity protein Tdi1 (Atu4351) from Agrobacterium tumefaciens
Lingling Shi, Zengqiang Gao, Tianyi Zhang, Heng Zhang and Yuhui Dong [1]
Molecular Tour
Structure of Type VI immunity protein Tdi1 (Atu4351) from Agrobacterium tumefaciens is composed a GAD-like domain inserted by a DUF1851 domain, and such domain organization is rare in known structures. There is a positive groove that is mainly located in the GAD-like domain that may be associated with nucleotide-binding.
. The GAD-like domain and the DUF1851 domain are shown in orange and cyan, respectively. The GAD-like domain structure is composed a seven-stranded twisted antiparallel β-sheet (β1↑-β2↓-β3↑-β4↓-β5↑-β6↓-β7↑) in the N-terminus and a two-stranded antiparallel β-sheet (β10↓-β11↑) in the C-terminus, surrounded by six helices (α1-α5 and η1). The DUF1851 domain is composed of a two-stranded antiparallel β-sheet (β8↓-β9↑) and four helices (η2-η3 and α6-α7). Therefore, the DUF1851 domain probably exists as an insertion of the GAD-like domain rather than an independent domain.
References
- ↑ Shi L, Gao Z, Zhang T, Zhang H, Dong Y. Crystal structure of the type VI immunity protein Tdi1 (Atu4351) from Agrobacterium tumefaciens. Acta Crystallogr F Struct Biol Commun. 2019 Mar 1;75(Pt 3):153-158. doi:, 10.1107/S2053230X19000815. Epub 2019 Feb 20. PMID:30839288 doi:http://dx.doi.org/10.1107/S2053230X19000815
