Year: 2018
Type: review
Abstract: The beta pore-forming proteins (β-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.
Source: Protein Science
DOI: 10.1002/pro.3454
Authors: Harry Scott, Wei Huang, James G. Bann, Derek J. Taylor
Institutions: Case Western Reserve University, Wichita State University
Language: English
Subfield: Structural Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $4,480
OpenAlex ID: W2888108436