A solution SAXS study of borrelia burgdorferi OspA, a protein containing a single‐layer β‐sheet
A solution SAXS study of borrelia burgdorferi OspA, a protein containing a single‐layer β‐sheet
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伯氏疏螺旋体 OspA（一种含有单层 β 片层的蛋白质）的溶液 SAXS 研究
DOI：
10.1002/pro.5560071223
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发表时间：
1998
期刊：
影响因子：
8
通讯作者：
S. Koide
中科院分区：
文献类型：
--
作者：
Z. Bu;D. Engelman;S. Koide
与单克隆抗体的Fab片段复合的伯氏疏螺旋体外表面蛋白A（OspA）的可溶性形式的晶体结构揭示了一种不寻常的结构，其具有重复的反平行β拓扑结构，其中非小叶单层β折叠连接球状N-和C-末端结构域。早期的NMR研究表明，OspA的局部结构（包括单层β折叠）与晶体结构相似。在这里，我们报告了一个小角X射线散射（SAXS）研究的整体构象的OspA在溶液中。用小角X射线散射（SAXS）法测得的溶液中OspA的回转半径（Rg）和长度分布函数（P（r））与晶体结构计算值基本一致。NMR和SAXS实验相互补充，表明包括中心单层β折叠的OspA在溶液中是稳定的结构，并且OspA晶体结构代表蛋白质的主要溶液构象。
The crystal structure of a soluble form of Borrelia burgdorferi outer surface protein A (OspA) complexed with the Fab fragment of a monoclonal antibody has revealed an unusual structure that has a repetitive antiparallel β topology with a nonglobular, single layer β‐sheet connecting the globular N‐ and C‐terminal domains. Earlier NMR studies have shown that the local structure of OspA including the single layer β‐sheet is similar to the crystal structure. Here we report a small angle X‐ray scattering (SAXS) study of the global conformation of OspA in solution. The radius of gyration (Rg) and the length distribution function (P(r)) of OspA measured by SAXS in solution are nearly identical to the calculated ones from the crystal structure, respectively. The NMR and SAXS experiments complement each other to show that OspA including the central single‐layer β‐sheet is a stable structure in solution, and that the OspA crystal structure represents the predominant solution conformation of the protein.