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Mechanochemistry of the kinesin 1 ATPase

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Figure

FIGURE 1Three states of the kinesin active site switch machinery. In the OPEN state (above),linking the switches is latched and the active site is hydrolytically-competent, with the lytic (W1)and proton-acceptor (W2) water molecules in position for nucleop
FIGURE 2The phosphate tube. Cartoon and spacefilling views of the catalytic center, withkinesin-5.ADP complex with STLC inhibitor.CLOSED state and the gamma phosphate and the Mgswitches colored as for Figure 1
FIGURE 3Neck linker docking and the coordination of molecularthe mechanism constraining the tethered head, it is clear that thewait-ATP state is pivotally important

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