Fig. 6: Conserved interactions of TreX-like toxins with thioredoxins.
From: Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin
a Cladogram of TreX toxin homologs (n = 2195). TreX-like (n = 1027) and Scabin-like (n = 707) clades are suggested based on the absence or the presence of potential disulfide bridge at the C-terminus respectively. b Structure of TreX (red) bound to TrxA (purple) is superimposed to the structure of the toxin Scabin (gray, PDB code: 6VV4). Scabin residues involved in disulfide bridge formation (C176 and C190) align with residues R118 and T130 of TreX, as shown in the zoom-in (right panel). c AlphaFold predicted models of TreX and Scabin-toxin homologs in complex with their cognate thioredoxins. X. bovienii complex (left, colored in red) was solved by X-ray crystallography and aligned to models of homologs from Pseudomonas spp. All AlphaFold prediction statistics are provided in Supplementary Fig. 11 and Supplementary Table 5. d Amino acid sequence alignments of TreX and Scabin toxin homologs. Active site residues are boxed in red, C-terminal extensions interacting with thioredoxins are boxed in blue, cysteines are highlighted in yellow.
