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

T N Pham; A Koide; S Koide

doi:10.1038/nsb0298-115

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

T N Pham·A Koide·S Koide

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Abstract

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.

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

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T N Pham, A Koide, S Koide. 1998. A stable single-layer beta-sheet without a hydrophobic core.. https://doi.org/10.1038/nsb0298-115

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