首页> 外文期刊>Journal of Molecular Biology >Confronting fusion protein-based membrane protein topology mapping with reality: the Escherichia coli ClcA H+/Cl- exchange transporter.
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Confronting fusion protein-based membrane protein topology mapping with reality: the Escherichia coli ClcA H+/Cl- exchange transporter.

机译:面对融合蛋白为基础的膜蛋白拓扑结构图与现实:大肠杆菌ClcA H + / Cl-交换转运蛋白。

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摘要

The topology of bacterial inner membrane proteins is commonly determined using topology reporters such as alkaline phosphatase and green fluorescent protein fused to a series of C-terminally truncated versions of the protein in question. Here, we report a detailed topology mapping of the Escherichia coli inner membrane H(+)/Cl(-) exchange transporter ClcA. Since the 3-D structure of ClcA is known, our results provide a critical test of the reporter fusion approach and offer new insights into the ClcA folding pathway.
机译:细菌内膜蛋白的拓扑结构通常是使用拓扑结构报告分子(例如碱性磷酸酶和绿色荧光蛋白)融合到相关蛋白的一系列C端截短形式来确定的。在这里,我们报告了大肠杆菌内膜H(+)/ Cl(-)交换转运蛋白ClcA的详细拓扑图。由于ClcA的3-D结构是已知的,我们的结果提供了对报告子融合方法的关键测试,并提供了有关ClcA折叠途径的新见解。

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