Three-dimensional structure of the insect (Lethocerus) flight muscle M-band.
The oval myosin filament profiles in transverse sections through the M-band of Lethocerus flight muscle are arranged in one of three orientations 60 degrees apart and point along the 11 directions of the hexagonal filament lattice. Relative orientations are not systematically related to give a superlattice structure, but neither are the orientations arranged completely randomly. In fact there is a nearly random structure with a slight bias towards adjacent filaments being identically oriented. This form of M-band structure is explained in terms of interactions between quasi-equivalent M-bridges. Its implications with regard to myosin crossbridge arrangement depend on the rotational symmetry of the crossbridge helix. For 6-stranded helices, 60 degrees rotations have no noticeable effect. However, in the case of the more likely 4-stranded structure, our results show that the crossbridge origins in the insect flight muscle A-band would be highly disordered. This disorder must be accounted for in interpreting both the flared-X crossbridge interactions seen in transverse sections of rigor insect flight muscle and the beautiful X-ray diffraction patterns from the same preparation. It is likely that in rigor insect muscle, some flared-Xs have the two heads of single myosin molecules interacting with two different actin filaments, whereas other flared-Xs have both of the myosin heads in one molecule interacting with the same actin filament.
D000818:Animals; D003599:Cytoskeleton / Q000648:ultrastructure; D006430:Hemiptera / Q000648:ultrastructure*; D008027:Light; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008961:Models, Structural; D009119:Muscle Contraction; D009126:Muscle Relaxation; D009210:Myofibrils / Q000648:ultrastructure*; D009218:Myosins; D012518:Sarcomeres / Q000648:ultrastructure*; D012542:Scattering, Radiation
D046911:Macromolecular Substances; D009218:Myosins