Myosin figure

When myosin is digested with trypsin, two myosin fragments (meromyosins) are generated. L ht mero-myosin (LMM) consists of aggregated, insoluble a-he-hcal fibers from the tail of myosin (Figure 49 ). LMM... 

The anatomical unit of muscle is an elongated cell called a fibre. Each individual fibre cell consists of myofibrils which are bundles of contractile protein filaments composed of actin and myosin (Figure 7.1). Differences in structure indicate that muscles have evolved to perform particular functions. Although the structure of fibres, myofibrils and filaments of actin and myosin, is similar in all muscle types, their arrangement, action and control allow identification of three tissue types ... 

Figure Bl.17.6. A protein complex (myosin SI decorated filamentous actin) embedded in a vitrified ice layer. Shown is a defociis series at (a) 580 mn, (b) 1130 mn, (c) 1700 mn and (d) 2600 mn underfocus. The pictures result from averagmg about 100 individual images from one electron micrograph the decorated filament length shown is 76.8 nm.

Figure Bl.17.12. Time-resolved visualization of the dissociation of myosin SI from filamentous actin (see also figure Bl.17.6). Shown are selected filament images before and after the release of a nucleotide analogue (AMPPNP) by photolysis (a) before flashing, (b) 20 ms, (c) 30 ms, (d) 80 ms and (e) 2 s after flashing. Note the change in obvious order (as shown by the diffraction insert in (a)) and the total dissociation of the complex in (e). The scale bar represents 35.4 mn. Picture with the courtesy of Academic Press.

Figure 14.10 A muscle viewed under the microscope is seen to contain many myofibrils that show a cross-striated appearance of alternating light and darkbands, arranged in repeating units called sarcomeres. The dark bands comprise myosin filaments and are interupted by M (middle) lines, which link adjacent myosin filaments to each other.

Figure 14.11 The sliding filament model of muscle contraction. The actin (red) and myosin (green) filaments slide past each other without shortening.

Figure 14.12 The swinging cross-bridge model of muscle contraction driven by ATP hydrolysis, (a) A myosin cross-bridge (green) binds tightly in a 45 conformation to actin (red), (b) The myosin cross-bridge is released from the actin and undergoes a conformational change to a 90 conformation (c), which then rebinds to actin (d). The myosin cross-bridge then reverts back to its 45° conformation (a), causing the actin and myosin filaments to slide past each other. This whole cycle is then repeated.

Figure 14.14 Sci ematic diagram of the myosin molecule, comprising two heavy chains (green) that form a coiled-coil tail with two globular heads and four light chains (gray) of two slightly differing sizes, each one bound to each heavy-chain globular head.

Figure 14.15 Stmcture of the SI fragment of chicken myosin as a Richardson diagram (a) and a space-filling model (b). The two light chains are shown in magenta and yellow. The heavy chain is colored according to three proteolytic fragments produced by trypsin a 25-kDa N-terminal domain (green) a central 50-kDa fragment (red) divided by a cleft into a 50K upper and a 50K lower domain and a 20-kDa C-terminal domain (blue) that links the myosin head to the coiled-coil tail. The 50-kDa and 20-kDa domains both bind actin, while the 25-kDa domain binds ATP. [(b) Courtesy of 1. Rayment.]...

It seems likely, therefore, that as the bound phosphate molecule is released, the cleft starts to open and the myosin head binds to actin (Figure 14.17d). Release of ADP coincides with a conformational change that fully opens the myosin cleft, causing actin to be tightly bound, and moves the lever arm to the "down" position. Since the myosin head is now strongly bound to actin at one end and covalently linked to the myosin fibril at the other... 

Figure 14.17 A sequence of events combining the swinging cross-bridge model of actin and myosin filament sliding with structural data of myosin with and without bound nucleotides.

FIGURE 17.17 All axial view of the two-stranded, a-helical coiled coll of a myosin tall. Hydrophobic residues a and d of the seven-resldne repeat sequence align to form a hydrophobic core. Residues b, c, and f face the outer surface of the colled coll and are typically Ionic. 

FIGURE 17.18 The packing of myosin molecules in a thick filament. Adjoining molecules are offset by approximately 14 nm, a distance corresponding to 98 residues of the coiled coil. 

FIGURE 17.21 A drawing of the arrangement of the elastic protein titin in the skeletal mnscle sarcomere. Titin filaments originate at the periphery of the M band and extend along the myosin filaments to the Z lines. These titin filaments produce the passive tension existing in myofibrils that have been stretched so that the thick and thin filaments no longer overlap and cannot interact. (Adapted from Ohtsuki, ., Maruyama, K, and Ebashi,. S ., 1986. Advances ia Protein Chemisti y 38 1—67.)... 

However, release of ADP and P from myosin is much slower. Actin activates myosin ATPase activity by stimulating the release of P and then ADP. Product release is followed by the binding of a new ATP to the actomyosin complex, which causes actomyosin to dissociate into free actin and myosin. The cycle of ATP hydrolysis then repeats, as shown in Figure 17.23a. The crucial point of this model is that ATP hydrolysis and the association and dissociation of actin and myosin are coupled. It is this coupling that enables ATP hydrolysis to power muscle contraction. 

FIGURE 17.23 The mechanism of skeletal muscle contraction. The free energy of ATP hydrolysis drives a conformational change in the myosin head, resulting in net movement of the myosin heads along the actin filament. Inset) A ribbon and space-filling representation of the actin—myosin interaction. (SI myosin image courtesy of Ivan Rayment and Hazel M. Holden, University of Wiseonsin, Madison.)... 

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