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. 1987 May;6(5):1475–1480. doi: 10.1002/j.1460-2075.1987.tb02389.x

The cell envelope of Thermoproteus tenax: three-dimensional structure of the surface layer and its role in shape maintenance

I Wildhaber 1, W Baumeister 1
PMCID: PMC553954  PMID: 16453767

Abstract

The sulphur-dependent archaebacterium Thermoproteus tenax has a cylindrical cell shape variable in length, but constant in diameter. Its whole surface is covered by a regular protein layer (S-layer). The lattice has p6 symmetry and a lattice constant of 32.8 nm. The three-dimensional reconstruction from a tilt series of isolated and negatively stained S-layer shows a complex mass distribution of the protein: a prominent, pillar-shaped protrusion is located at the 6-fold crystallographic axis with radiating arms connecting neighbouring hexamers in the vicinity of the 3-fold axis. The base vectors of the S-layer lattice have a preferred orientation with respect to the longitudinal axis of the cell. The layer can be seen as a helical structure consisting of a right-handed, two-stranded helix, with the individual chains running parallel. Supposing that new S-layer protein is inserted at lattice faults (wedge disclinations) near the poles, growing of the layer would then proceed by moving a disclination at the end of the helix. The constant shape of the cell, as well as the particular structure of the layer, strongly suggest that this S-layer has a shape-maintaining function.

Keywords: electron microscopy, S-layer, shape determination, Thermoproteus tenax, three-dimensional reconstruction

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Selected References

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