From in vitro towards in situ : structure‐based investigation of ABC exporters by electron paramagnetic resonance spectroscopy,FEBS Letters

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From in vitro towards in situ : structure‐based investigation of ABC exporters by electron paramagnetic resonance spectroscopy
FEBS Letters ( IF 3.0 ) Pub Date : 2020-12-01 , DOI: 10.1002/1873-3468.14004
Enrica Bordignon ₁ , Markus A. Seeger ₂ , Laura Galazzo ₁ , Gianmarco Meier ₂

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ATP‐binding cassette (ABC) exporters have been studied now for more than four decades, and recent structural investigation has produced a large number of protein database entries. Yet, important questions about how ABC exporters function at the molecular level remain debated, such as which are the molecular recognition hotspots and the allosteric couplings dynamically regulating the communication between the catalytic cycle and the export of substrates. This conundrum mainly arises from technical limitations confining all research to in vitro analysis of ABC transporters in detergent solutions or embedded in membrane‐mimicking environments. Therefore, a largely unanswered question is how ABC exporters operate in situ, namely in the native membrane context of a metabolically active cell. This review focuses on novel mechanistic insights into type I ABC exporters gained through a unique combination of structure determination, biochemical characterization, generation of conformation‐specific nanobodies/sybodies and double electron–electron resonance.

中文翻译：

从体外到原位：通过电子顺磁共振波谱对 ABC 输出体的结构研究

ATP 结合盒 (ABC) 输出器的研究已经超过 40 年，最近的结构研究产生了大量蛋白质数据库条目。然而，关于 ABC 输出蛋白如何在分子水平上发挥作用的重要问题仍然存在争议，例如哪些是分子识别热点和动态调节催化循环和底物输出之间通讯的变构偶联。这个难题主要源于技术限制，将所有研究限制在洗涤剂溶液中或嵌入膜模拟环境中的 ABC 转运蛋白的体外分析上。因此，一个很大程度上悬而未决的问题是 ABC 输出蛋白如何原位运作，即在代谢活跃细胞的天然膜环境中。

更新日期：2020-12-01

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