Skip to main content
Log in

A model of myosin crossbridge structure consistent with the low-angle X-ray diffraction pattern of vertebrate muscle

  • Papers
  • Published:
Journal of Muscle Research & Cell Motility Aims and scope Submit manuscript

Summary

Low-angle X-ray diffraction patterns have been taken of relaxed frog sartorius muscles stretched to destroy the lattice sampling in the pattern and the observed layer line pattern has been interpreted with model-building studies. The modelling calculations indicate that each crossbridge cannot be represented by a single cylindrical shape, but that the two S-1 heads of the crossbridge are tilted in opposite directions along the filament while twisted the same way round it so that the crossbridge lies wrapped round the filament backbone. The radial position derived for the crossbridge depends on how many strands the filament is assumed to have. If the filament is 2, 3 or 4 stranded then the centre of mass of the crossbridge lies at about 9.5, 12.5, or 15.5 nm respectively from the filament axis.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • FRANKLIN, R. E. & KLUG, A. (1955) The splitting of layer-lines in X-ray fibre diagrams of helical structures. Applications to tobacco mosaic virus.Acta. cryst. 8, 777–80.

    Google Scholar 

  • HASELGROVE, J. C. (1970)X-ray diffraction studies on muscles. Ph.D. dissertation. University of Cambridge, England.

    Google Scholar 

  • HASELGROVE, J. C. (1972) X-ray evidence for a conformational change in the actin containing filaments of vertebrate striated muscles.Cold Spring Harbor Symp. quant. Biol. 37, 341–52.

    Google Scholar 

  • HASELGROVE, J. C. (1975) X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle.J. molec. Biol. 92, 113–43.

    Google Scholar 

  • HASELGROVE, J. C. & HUXLEY, H. E. (1973) X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting muscle.J. molec. Bio. 77, 549–68.

    Google Scholar 

  • HUXLEY, H. E. (1952)X-ray diffraction studies of muscle. Ph.D. thesis, University of Cambridge.

  • HUXLEY, H. E. (1963) Electron microscope studies of the structure of natural and synthetic protein filaments from striated muscle.J. molec. Biol. 7, 281–308.

    Google Scholar 

  • HUXLEY, H. E. (1968) Structural difference between resting and rigor muscle; Evidence from intensity changes in the low-angle equatorial X-ray diagram.J. molec. Biol. 37, 507–20.

    Google Scholar 

  • HUXLEY, H. E. (1969) The mechanism of muscle contraction.Science 164, 1356–66.

    Google Scholar 

  • HUXLEY, H. E. & BROWN, W. (1967) The low angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor.J. molec. Biol. 30, 383–434.

    Google Scholar 

  • MILLER, A. & TREGEAR, R. T. (1972) Structure of insect fibrillar flight muscle in the presence and absence of ATP.J. molec. Biol. 70, 85–104.

    Google Scholar 

  • MOORE, P. B., HUXLEY, H. E. & De ROSIER, D. J. (1970) Three dimensional reconstruction of F actin thin filaments and decorated thin filaments.J. molec. Biol. 50, 279–95.

    Google Scholar 

  • MORIMOTO, K. & HARRINGTON, W. F. (1974) Substructure of thick filament of vertebrate striated muscle.J. molec. Biol. 83, 83–97.

    Google Scholar 

  • OFFER, G. & ELLIOTT, A. (1978) Can a myosin molecule bind to two actin filaments?Nature 271, 325–9.

    Google Scholar 

  • SQUIRE, J. M. (1972) General model of myosin filament structure.J. molec. Biol. 72, 125–38.

    Google Scholar 

  • SQUIRE, J. M. (1973) General model of myosin filament structure III. Molecular packing arrangements in myosin filaments.J. molec. Biol. 77, 291–323.

    Google Scholar 

  • SQUIRE, J. M. (1975) Muscle filament structure and muscle contraction.Ann. Rev. Biophys. Bioeng. 4, 137–63.

    Google Scholar 

  • SUTOH, K. & HARRINGTON, W. (1977) Cross linking of myosin filaments under activating and rigor conditions.Biochemistry 16, 2441–9.

    Google Scholar 

  • TREGEAR, R. T. & SQUIRE, J. M. (1973) Myosin content and filament structure in smooth and striated muscle.J. molec. Biol. 77, 279–90.

    Google Scholar 

  • VIBERT, P. J., HASELGROVE, J. C., LOWY, J. & POULSEN, F. R. (1972) Structural changes in actin-containing filaments of muscle.J. molec. Biol. 71, 757–67.

    Google Scholar 

  • WAKABAYASHI, T., HUXLEY, H. E., AMOS, L. A. & KLUG, A. (1975) Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin-T — troponin-I complex.J. molec. Biol. 93, 477–97.

    Google Scholar 

  • WRAY, J. S., VIBERT, P. J. & COHEN, C. (1975) Diversity of cross-bridge configurations in invertebrate muscles.Nature 257, 561–4.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Haselgrove, J.C. A model of myosin crossbridge structure consistent with the low-angle X-ray diffraction pattern of vertebrate muscle. J Muscle Res Cell Motil 1, 177–191 (1980). https://doi.org/10.1007/BF00711798

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00711798

Keywords

Navigation