A stable single-layer beta-sheet without a hydrophobic core

Nat Struct Biol. 1998 Feb;5(2):115-9. doi: 10.1038/nsb0298-115.


Outer surface protein A from the Lyme disease spirochete Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We show that the single-layer beta-sheet segment is surprisingly stable (deltaG for hydrogen exchange is approximately 8 kcal mol(-1) at 45 degrees C). Possible factors contributing to the stability of the single-layer beta-sheet are discussed based on an analysis of the crystal structure.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Surface / chemistry*
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Vaccines
  • Borrelia burgdorferi Group / chemistry*
  • Lipoproteins*
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary*


  • Antigens, Surface
  • Bacterial Outer Membrane Proteins
  • Bacterial Vaccines
  • Lipoproteins
  • OspA protein