Rich R L, Demeler B, Ashby K, Deivanayagam C C, Petrich J W, Patti J M, Narayana S V, Höök M
Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University, Houston 77030, USA.
Biochemistry. 1998 Nov 3;37(44):15423-33. doi: 10.1021/bi981773r.
Sequence analysis of surface proteins from Gram-positive bacteria indicates a composite organization consisting of unique and repeated segments. Thus, these proteins may contain discrete domains that could fold independently. In this paper, we have used a panel of biophysical methods, including gel permeation chromatography, analytical ultracentrifugation, circular dichroism, and fluorescence spectroscopy, to analyze the structural organization of the Staphylococcus aureus collagen adhesin, CNA. Our results indicate that the structure, function, and folding of the ligand-binding domain (A) are not affected by the presence or absence of the other major domain (B). In addition, little or no interaction is observed between the nearly identical repeat units within the B domain. We propose that CNA is indeed a mosaic protein in which the different domains previously indicated by sequence analysis operate independently.
革兰氏阳性菌表面蛋白的序列分析表明，其结构由独特和重复片段组成。因此，这些蛋白质可能包含可独立折叠的离散结构域。在本文中，我们使用了一系列生物物理方法，包括凝胶渗透色谱法、分析超速离心法、圆二色性和荧光光谱法，来分析金黄色葡萄球菌胶原蛋白黏附素CNA的结构组织。我们的结果表明，配体结合结构域（A）的结构、功能和折叠不受另一个主要结构域（B）存在与否的影响。此外，在B结构域内几乎相同的重复单元之间观察到很少或没有相互作用。我们认为CNA确实是一种镶嵌蛋白，其中先前通过序列分析指出的不同结构域独立发挥作用。
