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Publication Abstract from PubMed

Surface layers (S-layers) comprise the outermost cell envelope component of most archaea and many bacteria. Here we present the structure of the bacterial S-layer protein SbsC from Geobacillus stearothermophilus, showing a very elongated and flexible molecule, with strong and specific binding to the secondary cell wall polymer (SCWP). The crystal structure of rSbsC((31-844)) revealed a novel fold, consisting of six separate domains, which are connected by short flexible linkers. The N-terminal domain exhibits positively charged residues regularly spaced along the putative ligand binding site matching the distance of the negative charges on the extended SCWP. Upon SCWP binding, a considerable stabilization of the N-terminal domain occurs. These findings provide insight into the processes of S-layer attachment to the underlying cell wall and self-assembly, and also accommodate the observed mechanical strength, the polarity of the S-layer, and the pronounced requirement for surface flexibility inherent to cell growth and division.

The structure and binding behavior of the bacterial cell surface layer protein SbsC.,Pavkov T, Egelseer EM, Tesarz M, Svergun DI, Sleytr UB, Keller W Structure. 2008 Aug 6;16(8):1226-37. PMID:18682224^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.