NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer β-sheet

被引:28
作者
Pham, TN [1 ]
Koide, S [1 ]
机构
[1] Univ Rochester, Med Ctr, Dept Biochem & Biophys, Rochester, NY 14642 USA
关键词
Lyme disease; N-15 relaxation measurements; outer surface proteins; resonance assignments; beta-sheet; triple resonance NMR spectroscopy;
D O I
10.1023/A:1008246908142
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
The crystal structure of outer surface protein A (OspA) from 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 it is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We have accomplished nearly complete backbone H, C and N and C-beta/H-beta assignments of OspA (28 kDa) using standard triple resonance techniques without perdeuteration. This was made possible by recording spectra at a high temperature (45 degrees C). The chemical shift index and N-15 T-1/T-2 ratios show that both the secondary structure and the global conformation of OspA in solution are similar to the crystal structure, suggesting that the unique central beta-sheet is fairly rigid.
引用
收藏
页码:407 / 414
页数:8
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