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

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 (Delta G for hydrogen exchange is similar to 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.