ArticleThe Journal of biological chemistry2026
Self-assembly of surface layer protein SbsC from Geobacillus stearothermophilus and common principles of Bacilli S-layers.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
S-layers are (glyco)protein coats displayed on the external surface of many bacterial and archaeal species. By combining X-ray crystallography, electron cryo-tomography and SymProFold predictions, we propose the structure of the self-assembled S-layer protein (SLP) SbsC from the Gram-positive bacterium Geobacillus stearothermophilus ATCC 12980. SbsC consists of nine domains arranged like beads on a string. Domains 2 through 7 form a closed ring-like conformation, while the secondary cell wall polymer binding domain 1 and the auxiliary domains 8 and 9 protrude from the ring. Within the assembled lattice, the molecules adopt p1 symmetry and conform to the curvature of the bacterial surface, creating a sub-S-layer space, an enclosed space between the peptidoglycan layer and SLP lattice that may accommodate additional surface-associated proteins. Four Ca
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