Effects of adenosine diphosphate on the structure of myosin cross-bridges: an X-ray diffraction study on a single skinned frog muscle fibre.

Abstract

Using a technique to obtain a detailed X-ray diffraction pattern from a single skinned frog muscle fibre, we studied the effects of ADP on the structure and arrangement of myosin heads. An imaging plate and a cooled-CCD X-ray detector were used to record the diffraction patterns. Addition of 1 mM ADP to a rigor fibre increased the intensity of the third-order meridional reflection of the myosin repeat by 50-85%. The intensity of the sixth-order meridional reflection also increased. After removing the ADP, these intensities decreased but did not return to the level before the ADP was added. No significant changes were observed in the intensities of the equatorial reflections and the actin layer-lines. These results suggest that, upon ADP binding, the conformation of a myosin head changes without detaching from actin. The structural change may involve a relative motion between domains of the myosin head by the closure of the cleft to which an ADP molecule binds.