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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 FullText FullText_BOKU

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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