Cross-bridge conformation as revealed by x-ray diffraction studies on insect flight muscles with ATP analogues

The effects of three ATP analogues, alpha,beta-methylene-ATP [ATP(alpha,beta-CH1)], adenosine 5'-0-(3-thiotrophosphate) [ATP(gamma-S)], and beta,gamma-amino-ATP [ATP(beta,gamma-NH)] at various concentrations and temperatures on the X-ray fiber diagrams of glycerinated flight muscles from a wate...

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Bibliographic Details
Published in:Biophysical journal 1975-07, Vol.15 (7), p.687-705
Main Authors: Goody, R.S., Holmes, K.C., Mannherz, H.G., Leigh, J.B., Rosenbaum, G.
Format: Article
Language:English
Subjects:
Actins
Actomyosin
Adenosine Triphosphate - analogs & derivatives
Animals
Binding Sites
Flight, Animal
Glycerol
Insecta
Kinetics
Mathematics
Muscles - ultrastructure
Myosins
Protein Binding
Protein Conformation
Temperature
X-Ray Diffraction
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Summary:The effects of three ATP analogues, alpha,beta-methylene-ATP [ATP(alpha,beta-CH1)], adenosine 5'-0-(3-thiotrophosphate) [ATP(gamma-S)], and beta,gamma-amino-ATP [ATP(beta,gamma-NH)] at various concentrations and temperatures on the X-ray fiber diagrams of glycerinated flight muscles from a water bug (Lethocerus maximus) have been investigated. It is shown that the "relaxed" state can be obtained with all three analogues at high concentrations, the result being particularly clear with ATP(gamma-S). It is inferred that the binding of an ATP-like molecule suffices to produce the relaxed state. At low concentrations ATP(beta,gamma-NH) produces state intermediate between rigor and relaxed which is not simply a mixture of the two. The possible nature of the intermediate is discussed.
ISSN:0006-3495
1542-0086
DOI:10.1016/S0006-3495(75)85848-6