NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet

J Biomol NMR. 1998 May;11(4):407-14. doi: 10.1023/a:1008246908142.


The crystal structure of outer surface protein A (OspA) from 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 it is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We have accomplished nearly complete backbone H, C and N and C beta/H beta assignments of OspA (28 kDa) using standard triple resonance techniques without perdeuteration. This was made possible by recording spectra at a high temperature (45 degrees C). The chemical shift index and 15N T1/T2 ratios show that both the secondary structure and the global conformation of OspA in solution are similar to the crystal structure, suggesting that the unique central beta-sheet is fairly rigid.

MeSH terms

  • Antigens, Surface / chemistry*
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Vaccines
  • Borrelia burgdorferi Group / chemistry*
  • Carbon Isotopes
  • Isotope Labeling
  • Lipoproteins / chemistry*
  • Models, Molecular
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Structure, Secondary*


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