Three-dimensional reconstruction of thick filaments from Limulus and scorpion muscle.
We have produced three dimensional reconstructions, at a nominal resolution of 5 nm, of thick filaments from scorpion and Limulus skeletal muscle, both of which have a right-handed four-stranded helical arrangement of projecting subunits. In both reconstructions there was a distinct division of density within projecting subunits consistent with the presence of two myosin heads. Individual myosin heads appeared to be curved, with approximate dimensions of 16 X 5 X 5 nm and seemed more massive at one end. Our reconstructions were consistent with the two heads in a projecting subunit being arranged either antiparallel or parallel to each other and directed away from the bare zone. Although we cannot exclude the second of these interpretations, we favor the first as being more consistent with both filament models and also because it would enable easy phosphorylation of light chains. The antiparallel interpretation requires that the two heads within a subunit derive from different myosin molecules. In either interpretation, the two heads have different orientations relative to the thick filament shaft.
Stewart
M
M
Kensler
R W
RW
Levine
R J
RJ
D000818:Animals; D003201:Computers; D003599:Cytoskeleton / Q000648:ultrastructure*; D004577:Electron Probe Microanalysis; D006737:Horseshoe Crabs / Q000033:anatomy & histology*; D008954:Models, Biological; D009132:Muscles / Q000648:ultrastructure; D009218:Myosins; D009942:Organometallic Compounds; D012605:Scorpions / Q000033:anatomy & histology*; D013045:Species Specificity; D013194:Staining and Labeling; D014501:Uranium; D014961:X-Ray Diffraction
D009942:Organometallic Compounds; C005460:uranyl acetate; D014501:Uranium; D009218:Myosins