Fig. 1: Structural analysis of Trichuris suis BCL-2.
From: Diversity in the intrinsic apoptosis pathway of nematodes
a Overlay of CED-9 structures. In the structure of unbound CED-9 (PDB ID# 1OHU25, blue), the loop structure connecting helices α4 and α5 projects into the groove formed by helices α3 and α4. Upon binding EGL-1 (PDB ID# 1TY4 (ref. 26), pink), the loop undergoes a significant conformational change and is displaced from the groove, coincident with a reorientation and extension of helix α4 (T155-N158) with consequences for the interaction with CED-4. b Crystal structure of T. suis A. The protein adopts a helical bundle structure similar to other BCL-2 proteins (RMSD 2.4 Å over 141 residues versus BCL-XL (PDB 1PQ0); TM-score: 0.83303 (ref. 69)). Notable features include the entire α1 helix being visible, the well-defined α1–α2 loop and the long α8 helix. c The α4–α5 loop in CED-9 (blue) is not present in T. suis A (beige).
