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Related Experiment Videos

Is myosin a "back door" enzyme?

R G Yount1, D Lawson, I Rayment

  • 1Department of Biochemistry and Biophysics, Washington State University, Pullman 99164, USA.

Biophysical Journal
|April 1, 1995
PubMed
Summary
This summary is machine-generated.

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This study models adenosine triphosphate (ATP) in the myosin motor domain, revealing its active site positioning. This model explains ATP hydrolysis kinetics and myosin-ADP-vanadate complex formation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Muscle Physiology

Background:

  • Myosin motor proteins are crucial for muscle contraction.
  • Understanding the active site of myosin is key to elucidating ATP hydrolysis.
  • Previous models lacked detailed atomic positioning of ATP within the myosin active site.

Purpose of the Study:

  • To model adenosine triphosphate (ATP) within the active site of chicken skeletal myosin subfragment-1 (S1).
  • To rationalize existing experimental data on ATP analog binding and photolabeling.
  • To propose a mechanism for the release of inorganic phosphate (Pi) during the ATP hydrolysis cycle.

Main Methods:

  • Utilized the adenylate kinase.Ap5A structure as a reference for docking ATP into the S1 active site.
  • Analyzed the spatial arrangement of the ATP gamma-phosphate within the active site pocket.

Related Experiment Videos

  • Correlated the docked model with experimental photolabeling data from ATP analogs.

    • Main Results:

    • A docked structure of ATP.S1 was generated, consistent with photolabeling data.
    • The gamma-phosphate of ATP was localized to the bottom of the active site pocket.
    • A proposed mechanism suggests actin binding facilitates Pi release through a 'back-door' in the 50-kDa fragment.

    Conclusions:

    • The model provides a structural basis for understanding ATP hydrolysis by myosin.
    • The proposed Pi release mechanism explains key experimental observations, including hydrolysis kinetics and Pi exchange.
    • This work contributes to the understanding of the myosin ATPase cycle and muscle function.