A hypothesis about myosin catalysis

Hirofumi Onishi, Takashi Ohki, Naoki Mozhizuki, Manuel F. Morales

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)175-181
Number of pages7
JournalAdvances in Experimental Medicine and Biology
Volume538
Publication statusPublished - 2004
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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  • 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.