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Pore-forming protein toxins: from structure to function.

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TLDR
Recent work suggests a number of common features in the mechanism of membrane insertion may exist for each class of PFTs, and nearly all can be classified into one of two families based on the types of pores they are thought to form: alpha-P FTs or beta-PFTs.
Abstract
Pore-forming protein toxins (PFTs) are one of Nature's most potent biological weapons. An essential feature of their toxicity is the remarkable property that PFTs can exist either in a stable water-soluble state or as an integral membrane pore. In order to convert from the water-soluble to the membrane state, the toxin must undergo large conformational changes. There are now more than a dozen PFTs for which crystal structures have been determined and the nature of the conformational changes they must undergo is beginning to be understood. Although they differ markedly in their primary, secondary, tertiary and quaternary structures, nearly all can be classified into one of two families based on the types of pores they are thought to form: α-PFTs or β-PFTs. Recent work suggests a number of common features in the mechanism of membrane insertion may exist for each class.

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Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control.

TL;DR: Recent evidence suggests that Cyt synergize or overcome resistance to mosquitocidal-Cry proteins by functioning as a Cry-membrane bound receptor, and compares them to the mode of action of other bacterial PFT.
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MLKL Compromises Plasma Membrane Integrity by Binding to Phosphatidylinositol Phosphates

TL;DR: It is demonstrated that the full four-helical bundle domain (4HBD) in the N-terminal region of MLKL is required and sufficient to induce its oligomerization and trigger cell death, and found that a patch of positively charged amino acids on the surface of the 4HBD binds to phosphatidylinositol phosphates (PIPs) and allows recruitment ofMLKL to the plasma membrane.
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Bacillus thuringiensis insecticidal three‐domain Cry toxins: mode of action, insect resistance and consequences for crop protection

TL;DR: Activity of Cry1AMod toxins, which are able to form toxin oligomers in the absence of receptors, against different resistant populations, supports the hypothesis that toxin oligomerization is a limiting step in the Cry insecticidal activity.
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Staphylococcus aureus α-toxin: nearly a century of intrigue.

TL;DR: The identification of ADAM10 as a proteinaceous receptor for the toxin not only provides a greater appreciation of truths uncovered by many historic studies, but now affords the opportunity to more extensively probe and understand the role of α-toxin in modulation of the complex interaction of S. aureus with its human host.
References
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Journal ArticleDOI

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
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Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore

TL;DR: The structure proves the heptameric subunit stoichiometry of the α-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of β barrel pore-forming toxins.
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X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death.

TL;DR: The arrangement of the α-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphia toxin and the colicins, and may provide a clue to the mechanism of action of the B cl-2 family of proteins.
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Diversity of antimicrobial peptides and their mechanisms of action.

TL;DR: It is not likely that this diverse group of peptides has a single mechanism of action, but interaction of the peptides with membranes is an important requirement for most, if not all, antimicrobial peptides.
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Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores

TL;DR: It is concluded that, among naturally produced peptides that are investigated, only alamethicin conforms to the barrel-stave model, and other peptides, including magainins, melittin and protegrins, all appear to induce transmembrane pores that conform to the toroidal model.
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Recent work suggests a number of common features in the mechanism of membrane insertion may exist for each class.