Fig. 5

The ABD and Tox-GHH domain. a The Ten2 ABD and Tox-GHH domain are shown in surface representation and coloured as in Fig. 1b. The rest of the protein is shown as grey ribbons, oriented as in Fig. 1b. b Schematic of the ABD and Tox-GHH folds. The Tox-GHH area is indicated by a grey oval. Within the Tox-GHH, the TCAP area is shown in blue. Reported protease cleavage sites are indicated by arrowheads. c The ABD is shown as red ribbons. The shell surface is coloured white. The Tox-GHH domain is shown as white ribbons. d View of the Tox-GHH domain, coloured white except for the TCAP region, which is coloured in blue. The shell is shown as white surface, the ABD is shown as red ribbons. e View of the Tox-GHH domain as ribbons and the shell as surface. Residues are coloured according to the sequence conservation score of each residue (black = conserved, white = not conserved). Selected hydrophobic residues, all of which are conserved in Teneurins, are labelled and side chains shown as sticks (white from the TCAP area, blue from upstream Tox-GHH areas). f Overlay of the Ten2 Tox-GHH domain (red ribbon) and the nuclease domain of Colicin E9 (white ribbon, PDB 1BXI). Side chains of catalytically important residues are shown as sticks, and the catalytically important ion in Colicin E9 shown as a grey sphere. g Structure-based sequence alignment of the Escherichia coli DNase colicins, all four human Teneurin paralogues and chicken Ten2. The alignment corresponds to the most C-terminal two β-strands of the Ten2^CT crystal structure. The catalytically important residues of the Colicins are indicated by arrowheads. Each arrow corresponds to one β-strand