Advances in structure determination by cryo-EM to unravel membrane-spanning pore formation

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Authors
Scott, Harry
Huang, Wei
Bann, James G.
Taylor, Derek J.
Issue Date
2018-08-20
Type
Article
Language
en_US
Keywords
Cryo-EM , Membrane attack complex (MAC) , Cholesterol-dependent cytolysin (CDC) , Anthrax , Pore structure , Membrane
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Abstract

The beta pore-forming proteins (-PFPs) are a large class of polypeptides that are produced by all Kingdoms of life to contribute to their species' own survival. Pore assembly is a sophisticated multi-step process that includes receptor/membrane recognition and oligomerization events, and is ensued by large-scale structural rearrangements, which facilitate maturation of a prepore into a functional membrane spanning pore. A full understanding of pore formation, assembly, and maturation has traditionally been hindered by a lack of structural data; particularly for assemblies representing differing conformations of functional pores. However, recent advancements in cryo-electron microscopy (cryo-EM) techniques have provided the opportunity to delineate the structures of such flexible complexes, and in different states, to near-atomic resolution. In this review, we place a particular emphasis on the use of cryo-EM to uncover the mechanistic details including architecture, activation, and maturation for some of the prominent members of this family.

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This article is available under the terms of the Creative Commons Attribution License (CC BY) (which may be updated from time to time) and permits use, distribution and reproduction in any medium, provided that the Contribution is properly cited.
Citation
Scott, H. , Huang, W. , Bann, J. G. and Taylor, D. J. (2018), Advances in structure determination by cryo‐EM to unravel membrane‐spanning pore formation. Protein Science, 27: 1544-1556
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John Wiley and Sons
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ISSN
0961-8368
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