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

被引：47

作者：

Pham, TN ^{[1
]}

Koide, A ^{[1
]}

Koide, S ^{[1
]}

机构：

[1] Univ Rochester, Med Ctr, Dept Biochem & Biophys, Rochester, NY 14642 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1998年 / 5卷 / 02期

关键词：

D O I：

10.1038/nsb0298-115

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：115 / 119

页数：5

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