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Journal Article

Three-dimensional structure of the surface protein layer (MW layer) of Bacillus brevis 47

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Citation

Tsuboi, A., Engelhardt, H., Santarius, U., Tsukagoshi, N., Udaka, S., & Baumeister, W. (1989). Three-dimensional structure of the surface protein layer (MW layer) of Bacillus brevis 47. Journal of Ultrastructure & Molecular Structure Research., 102(2), 178-187.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-7497-7
Abstract
The three-dimensional (3D) structure of one surface protein layer from Bacillus brevis 47, the middle wall (MW) layer, has been reconstructed from tilted-view electron micrographs after correlation averaging to a resolution of 2 nm. The MW layer has p6 symmetry with a center-to-center spacing of 18.3 nm and a minimum thickness of 5.5 nm. The reconstruction reveals a distinct domain structure: the heavier domain of six monomers jointly forms a massive core centered at the sixfold symmetry axis, and lighter domains interconnect adjacent unit cells. In addition, the larger domains collectively form a pore by making contact with each other towards the inner surface, while the smaller domains establish a second connectivity towards the outer surface of the S layer. The MW layer of B. brevis resembles the S layer of Acetogenium kivui in various aspects: they have very similar lattice parameters and highly reminiscent 3D structures; the pores penetrate through the whole core and appear to determine the porosity of the S layers.