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Nucleotide-dependent shape changes in the reverse direction motor, myosin VI.

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  • 1Institute of Molecular and Cellular Biology, Leeds University, Leeds, UK.

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Myosin VI, an actin motor protein, changes shape dramatically upon nucleotide binding, adopting a pre-powerstroke conformation. This structural flexibility is crucial for its function in cellular processes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Myosin VI is a unique actin motor protein that moves towards the minus end of actin filaments.
  • Understanding its structural dynamics is key to elucidating its cellular roles.

Purpose of the Study:

  • To investigate the three-dimensional shape of myosin VI in various functional states using electron microscopy.
  • To compare the observed structures with existing crystal structures and understand nucleotide-induced conformational changes.

Main Methods:

  • Negative stain and metal shadow electron microscopy were employed to visualize myosin VI.
  • Single particle processing was utilized to generate high-resolution 2D averages of the molecular structures.
  • A large dataset of 169,964 particle images from different constructs and states was analyzed.

Main Results:

  • Myosin VI exhibits a bent conformation in its apo state, which changes significantly upon nucleotide binding (ATP, ADP, ATP-γS).
  • Nucleotide binding induces a straightening of the molecule and a large swing of the lever arm (∼140°).
  • The nucleotide-bound states resemble the pre-powerstroke conformation, contrary to expectations based on crystal structures.

Conclusions:

  • Myosin VI undergoes substantial conformational changes driven by nucleotide binding, adopting a pre-powerstroke-like state.
  • The full-length molecule exists primarily as a monomer, with potential regulation involving calmodulin light chains and calcium ions.
  • Electron microscopy reveals distinct structural features, including an extended tail structure under metal shadowing conditions.