The Structure and Binding Behavior of the Bacterial Cell Surface Layer Protein SbsC

Citations of this article
Mendeley users who have this article in their library.


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. © 2008 Elsevier Ltd. All rights reserved.

Author supplied keywords




Pavkov, T., Egelseer, E. M., Tesarz, M., Svergun, D. I., Sleytr, U. B., & Keller, W. (2008). The Structure and Binding Behavior of the Bacterial Cell Surface Layer Protein SbsC. Structure, 16(8), 1226–1237.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free