Journal:Acta Cryst F:S2053230X19000815
From Proteopedia
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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. | 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. | ||
| - | <scene name='80/806371/Cv/11'>Cartoon representation showing the domain architecture of Tdi1</scene>. 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 | + | <scene name='80/806371/Cv/11'>Cartoon representation showing the domain architecture of Tdi1</scene>. 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. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 11:33, 20 January 2019
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