Cryo-electron microscopy of cholinesterases, present and future,Journal of Neurochemistry

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Cryo-electron microscopy of cholinesterases, present and future
Journal of Neurochemistry ( IF 4.2 ) Pub Date : 2020-11-21 , DOI: 10.1111/jnc.15245
Miguel Ricardo Leung _{1,

2} , Tzviya Zeev-Ben-Mordehai _{1,

2}

Affiliation

Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) exist in a variety of oligomeric forms, each with defined cellular and subcellular distributions. Although crystal structures of AChE and BChE have been available for many years, structures of the physiologically relevant ChE tetramer were only recently solved by cryo-electron microscopy (cryo-EM) single-particle analysis. Here, we briefly review how these structures contribute to our understanding of cholinesterase oligomerization, highlighting the advantages of using cryo-EM to resolve structures of protein assemblies that cannot be expressed recombinantly. We argue that the next frontier in cholinesterase structural biology is to image membrane-anchored ChE oligomers directly in their native environment—the cell.

中文翻译：

胆碱酯酶的冷冻电子显微镜，现在和未来

乙酰胆碱酯酶 (AChE) 和丁酰胆碱酯酶 (BChE) 以多种寡聚形式存在，每种形式都有明确的细胞和亚细胞分布。尽管 AChE 和 BChE 的晶体结构已经存在多年，但生理相关 ChE 四聚体的结构最近才通过冷冻电子显微镜 (cryo-EM) 单粒子分析得到解决。在这里，我们简要回顾了这些结构如何有助于我们理解胆碱酯酶寡聚化，强调使用冷冻电镜解决无法重组表达的蛋白质组装结构的优势。我们认为胆碱酯酶结构生物学的下一个前沿是直接在细胞的天然环境中对膜锚定的 ChE 寡聚体进行成像。

更新日期：2020-11-21

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