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

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Abstract

Outer surface protein A from the Lyme disease spirochete Borrelia burgdorferi contains a single-layer (β-sheet connecting the N- and C-terminal globular domains. The central (β-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 (β-sheet segment is surprisingly stable (ΔG for hydrogen exchange is ∼8 kcal mol−1 at 45 °C). Possible factors contributing to the stability of the single-layer (β-sheet are discussed based on an analysis of the crystal structure.

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Authors and Affiliations

  1. Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York, 14642, USA

    Thúy-Nga Pham, Akiko Koide & Shohei Koide

Authors
  1. Thúy-Nga Pham
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  2. Akiko Koide
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  3. Shohei Koide
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Correspondence to Shohei Koide.

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Pham, TN., Koide, A. & Koide, S. A stable single-layer β-sheet without a hydrophobic core. Nat Struct Mol Biol 5, 115–119 (1998). https://doi.org/10.1038/nsb0298-115

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