NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
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.
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Department of Biochemistry and Biophysics, University of Rochester Medical Center, NY 14642, USA.
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D000954:Antigens, Surface / Q000737:chemistry*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D001428:Bacterial Vaccines; D015748:Borrelia burgdorferi Group / Q000737:chemistry*; D002247:Carbon Isotopes; D007553:Isotope Labeling; D008074:Lipoproteins / Q000737:chemistry*; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017433:Protein Structure, Secondary
D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; D002247:Carbon Isotopes; D008074:Lipoproteins; D009587:Nitrogen Isotopes; C072045:OspA protein