Comparison of the actomyosin-V interface within all three states (rigor: red; strong-ADP: orange; and AppNHp-bound post-rigor transition (PRT): purple). (
A, J) Overview of the central myosin molecule and the two actin subunits it is bound to (shades of green and blue, A
+1 and A
-1; for color code, see
Figure 1—figure supplement 3). (
B–I) Close-up views highlighting the localization and molecular details of all actin-myosin interfaces including the cardiomyopathy (CM) loop and loop 4 (
B–D), the helix-loop-helix (HLH) motif and activation loop (highlighted by an asterisk) (
D–G), loop 3 (
B, D, G, H), and loop 2 (
D, G, I). In close-up views of specific interfaces, the structure of the aged actomyosin-V complex in the rigor state is first shown on its own, followed by a superposition of all models illustrating the remarkable similarity of the actomyosin interface. Corresponding density maps are additionally shown as mesh (rigor: red; strong-ADP: orange; PRT: purple; and young rigor: gray). See
Figure 5 for residue labels and predicted hydrogen bonds.