Fig. 2

Three-dimensional structure of the wild-type (WT) and mutant kAE1 proteins. a Three-dimensional structure of wild-type kAE1 (blue) and superimposed structures of WT/SAO (blue/red), WT/T444N (blue/magenta), and SAO/T444N (red/magenta) as predicted by Swiss-model homology modeling server. b The protein structure where the SAO alteration is located. The deletion of residues 400–408 (green), which causes SAO, adversely affects the protein structure deletion and uncoiling of the helix (indicated by arrows). c The protein structure where the T444N alteration is located (indicated by arrows). There are two putative H-bonds connecting T444 (green) to L440 compared to only one putative H-bond connecting N444 (yellow) to L440. The dashed lines indicate the predicted H-bonds between residues