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.
| Original language | English |
|---|---|
| Pages (from-to) | 175-181 |
| Number of pages | 7 |
| Journal | Advances in Experimental Medicine and Biology |
| Volume | 538 |
| Publication status | Published - 2004 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Onishi, H., Ohki, T., Mozhizuki, N., & Morales, M. F. (2004). A hypothesis about myosin catalysis. Advances in Experimental Medicine and Biology, 538, 175-181.