Fig. 1: Architectures of substrate-free and substrate-bound human mitochondrial LONP1 protease.
From: Structures of the human LONP1 protease reveal regulatory steps involved in protease activation
a Lateral views of the substrate-free human LONP1 atomic model in a left-handed spiral configuration (center) flanked by axial exterior views of the ATPase (left) and protease (right) domain rings. Each subunit of the homohexamer is assigned a distinct color depending on its position in the spiral staircase, with the protease domains slightly desaturated in color relative to the ATPase domains. The same coloring is used throughout the figure. b The individual protomers of substrate-free human LONP1 lined up side-by-side, showing the ascending positions of the domains in the structure relative to the lowermost subunit. c Lateral views of the substrate-bound human LONP1 atomic model in a right-handed spiral configuration (center) flanked by axial exterior views of the ATPase (left) and protease (right) domain rings. The cryo-EM density of the substrate is shown as a solid isosurface colored orange. d The relative height of individual protomers within the substrate-bound conformer is shown by aligning all subunits to a common view, accentuated by dashed lines shown above the NTD3H.
