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

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Holmes,  Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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Mannherz,  Hans Georg
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Goody, R. S., Holmes, K. C., Mannherz, H. G., Barrington Leigh, J., & Rosenbaum, G. (1975). Cross-bridge conformation as revealed by x-ray diffraction studies on insect flight muscles with ATP analogues. Biophysical Journal, 15(7), 687-705. doi:10.1016/S0006-3495(75)85848-6.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-B152-3
Abstract
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.