Cryo-electron microscopy of cholinesterases, present and future

Miguel Ricardo Leung, Tzviya Zeev-Ben-Mordehai*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

Abstract

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. (Figure presented.).

Original languageEnglish
Pages (from-to)1236-1243
Number of pages8
JournalJournal of Neurochemistry
Volume158
Issue number6
Early online date21 Nov 2020
DOIs
Publication statusPublished - Sept 2021

Keywords

  • cholinesterase
  • cryo-electron microscopy
  • cryo-electron tomography

Fingerprint

Dive into the research topics of 'Cryo-electron microscopy of cholinesterases, present and future'. Together they form a unique fingerprint.

Cite this