Figure 8 | Scientific Reports

Figure 8

From: Starfish Apaf-1 activates effector caspase-3/9 upon apoptosis of aged eggs

Figure 8

Structure of human Apaf-1 WD40 repeat in complex with horse cytochrome c and the characteristics of the interface. (a) Amino acid residues in WD40 repeats of vertebrate Apaf-1 that interact with horse cytochrome c and the corresponding residues in sfApaf-1. The residue in gray background has the same type of amino acid as in human Apaf-1. Note that sfApaf-1 has a long deletion in each propeller domain compared with Apaf-1 of other animals. (b) The three-dimensional structure of human Apaf-1 (WD40 repeat region) in complex with horse cytochrome c (PDB ID: 3jbt chains A and B). WD40 repeat region is colored from green to red and cytochrome c in black. Amino acid residues in WD40 repeat that interact with cytochrome c are depicted in stick model. The interaction Structure of human Apaf-1 WD40 repeat in complex with horse cytochrome c and the characteristics of the interface. The interaction was calculated based on ∆accessiblity and chose the residues that have difference in solvent accessible area, when the protein interacts with the partner or not. Two loops in gray protruding from WD40 repeat to cytochrome c are deleted in sfApaf-1. (c) Percentage identity in WD40 repeats (blue) and that in cytochrome c binding residues (orange) between Apaf-1 of human and other animals. Note that the values of percentage identity reverse in starfish Apaf-1. (d) The amino acid sequence alignment of cytochrome c from animals. The sequences were obtained from UniPort and the ID is shown at the end of each sequence. The sequence identities are between 73 (starfish and human) and 100 (rat and mouse) %, which are much higher than those in WD40 repeat of Apaf-1.