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. 1981 Aug;78(8):4689–4693. doi: 10.1073/pnas.78.8.4689

Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell surface.

G N Phillips Jr, P F Flicker, C Cohen, B N Manjula, V A Fischetti
PMCID: PMC320228  PMID: 7029524

Abstract

The conformation and molecular dimensions of purified type 6 streptococcal M proteins establish the close structural relationship of these molecules to tropomyosin. Ultracentrifuge studies reveal that the M molecules exist as stable dimers; circular dichroism spectra indicate that the molecules contain about 70% alpha helix; and fiber x-ray diffraction diagrams show the characteristic reflections of the alpha-helical pattern. Electron microscopic images of M protein shadowed with platinum reveal rod-shaped molecules having the same width as tropomyosin. However, the lengths of the M molecules are about 30% shorter than lengths predicted by assuming a completely alpha-helical molecule. These findings indicate that the structure of the M6 protein is primarily alpha-helical coiled coil. Comparison of the lengths of the fibers on the surface of the streptococcus and the isolated M proteins suggests that each fiber on the cell wall consists of a single M-protein molecule approximately 500 A long. The structure determined for these fimbriae is the first alpha-helical coiled-coil conformation to be demonstrated for bacterial surface projections.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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