Fig. 7
From: Design of stable circular permutants of the GroEL chaperone apical domain
3D structure of AD-GroEL (PDB: 1DER, shown in grey) aligned with the structures of the circular permutants predicted by the AlphaFold program (colored with a color gradient located in the bottom of Figure). The wild-type protein structure is shown in grey. The orientation of the structures is the same in all subfigures. A Structure of AD-GroEL and cp211 circular permutant (least differing structures). B Structure of AD-GroEL and circular permutant cp256 (most differing structure). C-G – structural alignment of the six circular permutants with wild-type protein structure. The insets depict new N- (blue) and C- (green) terminal regions for each circular permutant. The orientation in the insets is optimized for a better view