Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

A hypothesis about myosin catalysis.

Hirofumi Onishi1, Takashi Ohki, Naoki Mozhizuki

  • 1Department of Structural Analysis, National Cardiovascular Center Research Institute, Suita, Osaka 565-8565.

Advances in Experimental Medicine and Biology
|April 22, 2004
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Estimating nasal nitric oxide from measured fractional exhaled nitric oxide and nasal fractional exhaled nitric oxide.

Journal of thoracic disease·2026
Same author

Long-Term Outcomes After Therapeutic Induction in Patients with Functional Dyspepsia.

Journal of clinical medicine·2025
Same author

The difference in tumor immune microenvironment and IFN-γ response between solid and non-solid adenocarcinoma.

Translational lung cancer research·2025
Same author

Single-cell sequencing on CD8<sup>+</sup> TILs revealed the nature of exhausted T cells recognizing neoantigen and cancer/testis antigen in non-small cell lung cancer.

Journal for immunotherapy of cancer·2023
Same author

Identification and characterization of LPLAT7 as an sn-1-specific lysophospholipid acyltransferase.

Journal of lipid research·2022
Same author

Abnormal male reproduction and embryonic development induced by downregulation of a phospholipid fatty acid-introducing enzyme Lpgat1 in zebrafish.

Scientific reports·2022

Myosin head movement relies on ATP binding, causing conformational changes. Site-directed mutagenesis revealed Arg247 and Glu470 residues are crucial for ATP hydrolysis and muscle contraction.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Muscle Physiology

Background:

  • Myosin heads undergo conformational changes upon adenosine triphosphate (ATP) binding, leading to muscle contraction.
  • A salt-bridge forms between Glu470 (Switch II) and Arg247 (Switch I) in the closed state of the myosin active site.
  • Understanding the roles of these specific residues is key to elucidating the mechanism of ATP hydrolysis in muscle function.

Purpose of the Study:

  • To investigate the functional significance of the Arg247-Glu470 salt-bridge in myosin.
  • To determine the role of Arg247 in ATP binding-induced cleft closure.
  • To clarify the involvement of Glu470 in the positioning of water during ATP hydrolysis.

Main Methods:

  • Site-directed mutagenesis was employed to alter the bridging residues Arg247 and Glu470.

Related Experiment Videos

  • The functional consequences of these mutations on myosin head conformation and ATP hydrolysis were analyzed.

    • Main Results:

    • The attractive force between Arg247 and the gamma-phosphate of ATP was shown to drive cleft closure.
    • Glu470 was found to be critical for orienting the lytic water molecule for nucleophilic attack on the gamma-phosphorus during hydrolysis.
    • Evidence suggests the salt-bridge formation is intrinsically linked to the hydrolysis reaction.

    Conclusions:

    • The Arg247-Glu470 salt-bridge plays a pivotal role in both the mechanical steps of myosin function and the chemical process of ATP hydrolysis.
    • Arg247 is essential for the conformational change leading to cleft closure upon ATP binding.
    • Glu470 is directly involved in the catalytic step of ATP hydrolysis by facilitating water attack.