TY - JOUR
T1 - Cryo-electron microscopy of cholinesterases, present and future
AU - Leung, Miguel Ricardo
AU - Zeev-Ben-Mordehai, Tzviya
N1 - Funding Information:
We thank the organizers of the 16th International Symposium on Cholinergic Mechanisms for giving us the opportunity to write this article. MRL is supported by a Clarendon Fund—Nuffield Department of Medicine Prize Studentship.
Funding Information:
We thank the organizers of the 16th International Symposium on Cholinergic Mechanisms for giving us the opportunity to write this article. MRL is supported by a Clarendon Fund?Nuffield Department of Medicine Prize Studentship.
Publisher Copyright:
© 2020 The Authors. Journal of Neurochemistry published by John Wiley & Sons Ltd on behalf of International Society for Neurochemistry
PY - 2021/9
Y1 - 2021/9
N2 - 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.).
AB - 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.).
KW - cholinesterase
KW - cryo-electron microscopy
KW - cryo-electron tomography
UR - http://www.scopus.com/inward/record.url?scp=85097495335&partnerID=8YFLogxK
U2 - 10.1111/jnc.15245
DO - 10.1111/jnc.15245
M3 - Review article
C2 - 33222205
AN - SCOPUS:85097495335
SN - 0022-3042
VL - 158
SP - 1236
EP - 1243
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
IS - 6
ER -