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November 1, 1989The Journal of Biochemistry

The Effects of Various Nucleotides on the Structure of Actin-Attached Myosin Subfragment-1 Studied by Quick-Freeze Deep-Etch Electron Microscopy1

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Population

Native acto-S1 (actin-attached myosin subfragment-1) and covalently cross-linked acto-S1

Comparison

Addition of various nucleotides vs Rigor conditions (no ATP)

Design

Preclinical

Authors

EKEisaku KatayamaChiba University Hospital

Discussion

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Implication

Premature for clinical translation in myosin-targeted therapies; leaves open conformational dynamics in human cardiac cross-bridge cycling.

Structured PICO

P
Population
Native acto-S1 (actin-attached myosin subfragment-1) and covalently cross-linked acto-S1
I
Intervention
Addition of various nucleotides (ATP, ADP, ADP-inorganic vanadate, Adenyl-5'-yl imidodiphosphate, inorganic pyrophosphate)
C
Comparator
Rigor conditions (no ATP)
O
Outcome
Structural changes of myosin heads (S1) attached to actinsurrogate

This basic science study demonstrates that myosin heads undergo distinct structural changes, becoming short and round, upon the addition of ATP or ADP-inorganic vanadate.

Cite This Study

Eisaku Katayama (1989) studied this question.

synapsesocial.com/papers/6a8586404f2eb4dbc91e6079https://doi.org/10.1093/oxfordjournals.jbchem.a122928
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Time-resolved electron microscopic analysis of the behavior of myosin heads on actin filaments after photolysis of caged ATP.1993 · 17 citations
  2. 2Structure of the actin-myosin complex in the presence of ATP.1985 · 81 citations
  3. 3New states of actomyosin.1987 · 45 citations
  4. 4Effect of ATP Analogues on the Actin−Myosin Interface1998 · 20 citations
  5. 5The conformation of cross-linked actin·S-1 in the presence and absence of ATP.1987 · 12 citations