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Three-dimensional structure of the surface protein layer (MW layer) of Bacillus brevis 47
Institution:1. China Merchants Chongqing Communications Research & Design Institute Co., Ltd, Chongqing, China;2. School of Civil Engineering, Chongqing Jiaotong University, Chongqing, China;3. Institute of Rock and Soil Mechanics, Chinese Academy of Sciences, Wuhan, China;4. Guangdong University of Technology, Guangzhou, China;1. Bio-Protection Research Centre, PO Box 85084, Lincoln University, Lincoln, New Zealand;2. Cardiff School of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, UK;3. Universidad Nacional de Villa María, Instituto A.P. de Ciencias Básicas y Aplicadas, Av. Arturo Jauretche 1555, Villa María 5900, Córdoba, Argentina;4. Statistics and Bioinformatics Group, Institute of Fundamental Sciences, Massey University, Palmerston North 4410, New Zealand
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.
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