Structural and Functional Analysis of the S-Layer Protein from Bacillus stearothermophilus

  • Beatrix Kuen
  • Werner Lubitz
  • Geoffrey J. Barton
Chapter
Part of the NATO ASI Series book series (NSSA, volume 252)

Abstract

One feature common to many bacteria, regardless of their phylogenetic origin within the kingdoms Eucarya or Archaea, is the presence of a regularly ordered (glyco)protein border as the outermost macromolecular layer of the cell envelope. A recent list of organisms with such crystalline surface layers (S-layers) cites approximately 300 different prokaryotic species (Messner and Sleytr, 1992). However, most of the S-layers have only been described by electron microscopical or biochemical investigations and DNA sequence data of the corresponding genes are available for very few species (approximately 20). Here we report on the structural and functional properties of the S-layer of Bacillus stearothermophilus strain PV72 which have been deduced from computer analysis of DNA-sequence data (for sequencing details of the gene see the contribution by Kuen, Sára, Sleytr, and Lubitz in this book).

Keywords

Cell Wall Protein Bacillus Stearothermophilus Prokaryotic Species Protein Multiple Sequence Alignment Strain PV72 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Beatrix Kuen
    • 1
  • Werner Lubitz
    • 1
  • Geoffrey J. Barton
    • 2
  1. 1.Institute of Microbiology and GeneticsUniversity of ViennaViennaAustria
  2. 2.Laboratory of Molecular BiophysicsUniversity of OxfordOxfordEngland

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