Abstract
When ATP binds to the active site of myosin heads, Switch II undergoes a large conformational change and the cleft surrounding the bound γ-phosphate closes. In the closed state, Glu470 in Switch II comes together with Arg247 in Switch I to form a salt-bridge. Here, the functional significance of the two bridging residues was tested by using site-directed mutagenesis. We conclude from such tests that (a) the attractive force between Arg247 and the γ-phosphate of ATP moves the cleft to close, and (b) during hydrolysis, Glu470 is intimately involved in positioning the lytic water for the attack on the γ-phosphorus. We also speculate on how the salt-bridge between Arg247 and Glu470 is related to hydrolysis.
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Onishi, H., Ohki, T., Mozhizuki, N., Morales, M.F. (2003). A Hypothesis About Myosin Catalysis. In: Sugi, H. (eds) Molecular and Cellular Aspects of Muscle Contraction. Advances in Experimental Medicine and Biology, vol 538. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9029-7_16
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DOI: https://doi.org/10.1007/978-1-4419-9029-7_16
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