Journal:Acta Cryst F:S2053230X19000815
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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). 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. | + | <scene name='80/806371/Cv/11'>Cartoon representation showing the domain architecture of Tdi1</scene> (PDB ID [[6itw]]). 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. |
<scene name='80/806371/Cv/14'>The spacefill representation of Tdi1</scene> (blue, positive; red, negative), colored by its local electrostatic potential. Remarkably, there is a groove that is mainly composed of β7, η1 and α5 in the GAD-like domain and extends to β8 in theDUF1851 domain. Many of the residues constituting the groove are conserved or highly conserved among Tdi1 homologs. Inspection of the surface charge distribution of the groove revealed it is covered with dominantly positive charges, which may be associated with nucleotide-binding. | <scene name='80/806371/Cv/14'>The spacefill representation of Tdi1</scene> (blue, positive; red, negative), colored by its local electrostatic potential. Remarkably, there is a groove that is mainly composed of β7, η1 and α5 in the GAD-like domain and extends to β8 in theDUF1851 domain. Many of the residues constituting the groove are conserved or highly conserved among Tdi1 homologs. Inspection of the surface charge distribution of the groove revealed it is covered with dominantly positive charges, which may be associated with nucleotide-binding. | ||
Revision as of 13:24, 11 May 2022
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