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Nat Struct Biol. 1998 Feb;5(2):115-9.

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

Author information

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

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.

PMID:
9461076
[Indexed for MEDLINE]

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