BOKU - Universität für Bodenkultur Wien - Forschungsinformationssystem
Gewählte Publikation:
Pavkov, T; Egelseer, EM; Tesarz, M; Svergun, DI; Sleytr, UB; Keller, W.
(2008):
The structure and binding behavior of the bacterial cell surface layer protein SbsC.
Structure. 2008; 16(8):1226-1237
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- Abstract:
- Surface layers (S-layers) comprise the outermost cell envelope component of most archaea and many bacteria. Here we present the structure of the bacteria[ 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 selfassembly, 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.
- Autor*innen der BOKU Wien:
- Egelseer Eva Maria
- Sleytr Uwe B.
- Find related publications in this database (using NML MeSH Indexing)
- Bacillus stearothermophilus - chemistry
- Bacterial Proteins - chemistry
- Binding Sites -
- Crystallography, X-Ray -
- Membrane Proteins - chemistry
- Models, Molecular -
- Molecular Sequence Data -
- Protein Binding -
- Protein Folding -
- Protein Structure, Secondary -
- Protein Structure, Tertiary -
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