An actin-dependent conformational change in myosin

Ming Xiao, Jeff G. Reifenberger, Amber L. Wells, Corry Baldacchino, Li Qiong Chen, Pinghua Ge, H. Lee Sweeney, Paul R. Selvin

Research output: Contribution to journalArticle

Abstract

Conformational changes within myosin lead to its movement relative to an actin filament. Several crystal structures exist for myosin bound to various nucleotides, but none with bound actin. Therefore, the effect of actin on the structure of myosin is poorly understood. Here we show that the swing of smooth muscle myosin lever arm requires both ADP and actin. This is the first direct observation that a conformation of myosin is dependent on actin. Conformational changes within myosin were monitored using fluorescence resonance energy transfer techniques. A cysteine-reactive probe is site-specifically labeled on a 'cysteine-light' myosin variant, in which the native reactive cysteines were removed and a cysteine engineered at a desired position. Using this construct, we show that the actin-dependent ADP swing causes an 18 Å change in distance between a probe on the 25/50 kDa loop on the catalytic domain and a probe on the regulatory light chain, corresponding to a 23° swing of the light-chain domain.

Original languageEnglish (US)
Pages (from-to)402-408
Number of pages7
JournalNature Structural Biology
Volume10
Issue number5
DOIs
StatePublished - May 1 2003

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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    Xiao, M., Reifenberger, J. G., Wells, A. L., Baldacchino, C., Chen, L. Q., Ge, P., Sweeney, H. L., & Selvin, P. R. (2003). An actin-dependent conformational change in myosin. Nature Structural Biology, 10(5), 402-408. https://doi.org/10.1038/nsb916