2RA1

Crystal structure of the N-terminal part of the bacterial S-layer protein SbsC

Summary for 2RA1

• Entry DOI: 10.2210/pdb2ra1/pdb
• Descriptor: Surface layer protein (2 entities in total)
• Functional Keywords: triple coiled-coil, s-layer protein, protein binding, sugar binding protein
• Biological source: Geobacillus stearothermophilus (Bacillus stearothermophilus)
• Total number of polymer chains: 1
• Total formula weight: 45051.75

Authors

Pavkov, T.,Egelseer, E.M.,Tesarz, M.,Sleytr, U.B.,Keller, W. (deposition date: 2007-09-14, release date: 2008-08-19, Last modification date: 2024-02-21)

Primary citation

Pavkov, T.,Egelseer, E.M.,Tesarz, M.,Svergun, D.I.,Sleytr, U.B.,Keller, W.
The structure and binding behavior of the bacterial cell surface layer protein SbsC.
Structure, 16:1226-1237, 2008

PubMed Abstract: 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.

PubMed: 18682224
DOI: 10.1016/j.str.2008.05.012

Experimental method

X-RAY DIFFRACTION (2.406 Å)