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Comment
. 1998 Mar 17;95(6):2720-2.
doi: 10.1073/pnas.95.6.2720.

New angle on myosin

Affiliations
Comment

New angle on myosin

R Cooke. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Figure 1
Figure 1
A model of the actomyosin complex illustrates how the spectroscopic results described by Baker et al. (6) might translate into the domain movements of myosin. The actin filament is shown in purple on the left. The catalytic domain of the myosin head, shown in red, attaches rigidly to the actin filament, with its light chain domain extending down at about a 45° angle. The two light chains that help form this domain are shown in white and cyan, with the spectroscopic label of Baker et al. (6) attached to the latter. The light chain domain is also shown in a second orientation in blue, rotated upward by approximately 36° to simulate the beginning of the power stroke suggested by the results of Baker et al. (6). The power stroke would consist of a rotation of this domain from the upper position to the lower. This rotation would pull the tether that connects the myosin head to the thick filament, down by about 5 nm. The position of the tether is depicted schematically by the thick black vertical lines. The model is derived from the coordinates of the crystal structures and displayed in Midas (–10).

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